Identification of the Babesia-responsive leucine-rich repeat domain-containing protein from the hard tick Haemaphysalis longicornis

Haemaphysalis longicornis is a tick known for transmitting Babesia parasites, including Babesia gibsoni, in East Asian countries. The vector tick must have strategies to control Babesia parasites, while Babesia parasites are also considered to establish an evasive mechanism from the tick’s innate im...

Full description

Saved in:
Bibliographic Details
Published inParasitology research (1987) Vol. 114; no. 5; pp. 1793 - 1802
Main Authors Maeda, Hiroki, Kurisu, Koshi, Miyata, Takeshi, Kusakisako, Kodai, Galay, Remil Linggatong, Rio, Talactac Melbourne, Mochizuki, Masami, Fujisaki, Kozo, Tanaka, Tetsuya
Format Journal Article
LanguageEnglish
Published Berlin/Heidelberg Springer-Verlag 01.05.2015
Springer Berlin Heidelberg
Springer
Subjects
Online AccessGet full text

Cover

Loading…
Abstract Haemaphysalis longicornis is a tick known for transmitting Babesia parasites, including Babesia gibsoni, in East Asian countries. The vector tick must have strategies to control Babesia parasites, while Babesia parasites are also considered to establish an evasive mechanism from the tick’s innate immunity. Due to this mutual tolerance, H. longicornis is considered to be a vector of Babesia parasites. Recent studies have shown the important roles of leucine-rich repeat (LRR) domain-containing proteins in innate immunity in many living organisms. Some LRR domain-containing proteins were identified in ticks; however, their functions are still unknown. In this study, a novel LRR domain-containing protein was identified from H. longicornis (HlLRR). HlLRR contains two LRR domains, and the expression levels of mRNA and proteins were upregulated during blood feeding, particularly in the salivary glands and midgut. In addition, recombinant HlLRR (rHlLRR) demonstrated growth inhibition activity against B. gibsoni in vitro without a hemolytic effect at any concentration used. Moreover, the diameters of Babesia merozoites treated with rHlLRR were significantly larger than those of the control group. These results strongly indicate the key roles of HlLRR in the tick’s innate immunity against Babesia parasites. Furthermore, HlLRR might be a potential alternative drug to treat babesiosis.
AbstractList Haemaphysalis longicornis is a tick known for transmitting Babesia parasites, including Babesia gibsoni , in East Asian countries. The vector tick must have strategies to control Babesia parasites, while Babesia parasites are also considered to establish an evasive mechanism from the tick’s innate immunity. Due to this mutual tolerance, H. longicornis is considered to be a vector of Babesia parasites. Recent studies have shown the important roles of leucine-rich repeat (LRR) domain-containing proteins in innate immunity in many living organisms. Some LRR domain-containing proteins were identified in ticks; however, their functions are still unknown. In this study, a novel LRR domain-containing protein was identified from H. longicornis (HlLRR). HlLRR contains two LRR domains, and the expression levels of mRNA and proteins were upregulated during blood feeding, particularly in the salivary glands and midgut. In addition, recombinant HlLRR (rHlLRR) demonstrated growth inhibition activity against B. gibsoni in vitro without a hemolytic effect at any concentration used. Moreover, the diameters of Babesia merozoites treated with rHlLRR were significantly larger than those of the control group. These results strongly indicate the key roles of HlLRR in the tick’s innate immunity against Babesia parasites. Furthermore, HlLRR might be a potential alternative drug to treat babesiosis.
Haemaphysalis longicornis is a tick known for transmitting Babesia parasites, including Babesia gibsoni, in East Asian countries. The vector tick must have strategies to control Babesia parasites, while Babesia parasites are also considered to establish an evasive mechanism from the tick's innate immunity. Due to this mutual tolerance, H. longicornis is considered to be a vector of Babesia parasites. Recent studies have shown the important roles of leucine-rich repeat (LRR) domain-containing proteins in innate immunity in many living organisms. Some LRR domain-containing proteins were identified in ticks; however, their functions are still unknown. In this study, a novel LRR domain-containing protein was identified from H. longicornis (HlLRR). HlLRR contains two LRR domains, and the expression levels of mRNA and proteins were upregulated during blood feeding, particularly in the salivary glands and midgut. In addition, recombinant HlLRR (rHlLRR) demonstrated growth inhibition activity against B. gibsoni in vitro without a hemolytic effect at any concentration used. Moreover, the diameters of Babesia merozoites treated with rHlLRR were significantly larger than those of the control group. These results strongly indicate the key roles of HlLRR in the tick's innate immunity against Babesia parasites. Furthermore, HlLRR might be a potential alternative drug to treat babesiosis.
Haemaphysalis longicornis is a tick known for transmitting Babesia parasites, including Babesia gibsoni, in East Asian countries. The vector tick must have strategies to control Babesia parasites, while Babesia parasites are also considered to establish an evasive mechanism from the tick's innate immunity. Due to this mutual tolerance, H. longicornis is considered to be a vector of Babesia parasites. Recent studies have shown the important roles of leucine-rich repeat (LRR) domain-containing proteins in innate immunity in many living organisms. Some LRR domain-containing proteins were identified in ticks; however, their functions are still unknown. In this study, a novel LRR domain-containing protein was identified from H. longicornis (HlLRR). HlLRR contains two LRR domains, and the expression levels of mRNA and proteins were upregulated during blood feeding, particularly in the salivary glands and midgut. In addition, recombinant HlLRR (rHlLRR) demonstrated growth inhibition activity against B. gibsoni in vitro without a hemolytic effect at any concentration used. Moreover, the diameters of Babesia merozoites treated with rHlLRR were significantly larger than those of the control group. These results strongly indicate the key roles of HlLRR in the tick's innate immunity against Babesia parasites. Furthermore, HlLRR might be a potential alternative drug to treat babesiosis.Haemaphysalis longicornis is a tick known for transmitting Babesia parasites, including Babesia gibsoni, in East Asian countries. The vector tick must have strategies to control Babesia parasites, while Babesia parasites are also considered to establish an evasive mechanism from the tick's innate immunity. Due to this mutual tolerance, H. longicornis is considered to be a vector of Babesia parasites. Recent studies have shown the important roles of leucine-rich repeat (LRR) domain-containing proteins in innate immunity in many living organisms. Some LRR domain-containing proteins were identified in ticks; however, their functions are still unknown. In this study, a novel LRR domain-containing protein was identified from H. longicornis (HlLRR). HlLRR contains two LRR domains, and the expression levels of mRNA and proteins were upregulated during blood feeding, particularly in the salivary glands and midgut. In addition, recombinant HlLRR (rHlLRR) demonstrated growth inhibition activity against B. gibsoni in vitro without a hemolytic effect at any concentration used. Moreover, the diameters of Babesia merozoites treated with rHlLRR were significantly larger than those of the control group. These results strongly indicate the key roles of HlLRR in the tick's innate immunity against Babesia parasites. Furthermore, HlLRR might be a potential alternative drug to treat babesiosis.
Haemaphysalis longicornis is a tick known for transmitting Babesia parasites, including Babesia gibsoni, in East Asian countries. The vector tick must have strategies to control Babesia parasites, while Babesia parasites are also considered to establish an evasive mechanism from the tick's innate immunity. Due to this mutual tolerance, H. longicornis is considered to be a vector of Babesia parasites. Recent studies have shown the important roles of leucine-rich repeat (LRR) domain-containing proteins in innate immunity in many living organisms. Some LRR domain-containing proteins were identified in ticks; however, their functions are still unknown. In this study, a novel LRR domain-containing protein was identified from H. longicornis (HlLRR). HlLRR contains two LRR domains, and the expression levels of mRNA and proteins were upregulated during blood feeding, particularly in the salivary glands and midgut. In addition, recombinant HlLRR (rHlLRR) demonstrated growth inhibition activity against B. gibsoni in vitro without a hemolytic effect at any concentration used. Moreover, the diameters of Babesia merozoites treated with rHlLRR were significantly larger than those of the control group. These results strongly indicate the key roles of HlLRR in the tick's innate immunity against Babesia parasites. Furthermore, HlLRR might be a potential alternative drug to treat babesiosis. Electronic supplementary material The online version of this article (doi:10.1007/s00436-015-4365-7) contains supplementary material, which is available to authorized users.
Audience Academic
Author Fujisaki, Kozo
Kusakisako, Kodai
Rio, Talactac Melbourne
Tanaka, Tetsuya
Maeda, Hiroki
Galay, Remil Linggatong
Mochizuki, Masami
Kurisu, Koshi
Miyata, Takeshi
Author_xml – sequence: 1
  fullname: Maeda, Hiroki
– sequence: 2
  fullname: Kurisu, Koshi
– sequence: 3
  fullname: Miyata, Takeshi
– sequence: 4
  fullname: Kusakisako, Kodai
– sequence: 5
  fullname: Galay, Remil Linggatong
– sequence: 6
  fullname: Rio, Talactac Melbourne
– sequence: 7
  fullname: Mochizuki, Masami
– sequence: 8
  fullname: Fujisaki, Kozo
– sequence: 9
  fullname: Tanaka, Tetsuya
BackLink https://www.ncbi.nlm.nih.gov/pubmed/25690462$$D View this record in MEDLINE/PubMed
BookMark eNqNks1u1DAUhSNURKeFB2ADltiwSbFjx06WbdXSSpVYQNfWjXM945LYg-1B6poXx9MUJBCqkBfXsr7j-3eOqgMfPFbVa0ZPGKXqQ6JUcFlT1tYltrV6Vq2Y4E3N-rY9qFa0L3fKGD-sjlK6o5QpKcSL6rBpZU-FbFbVj-sRfXbWGcgueBIsyRskZzBgclBHTNvgk_uOZMKdcR7r6MyGRNwiZDKGGZyvTfC5ROfXZBtDRueJjWF--GkDcSTZma_kCnCG7eY-weQSmYJfOxOid-ll9dzClPDVYzyubi8vvpxf1TefPl6fn97URlKRa5AAnRl7blULOLJBSCU4U6KVYuB9Z0CIRqhBmG6U3NqWMYtgbTMoHArJj6v3y7-lyG87TFnPLhmcJvAYdkkz2UlFecfVf6CKc8X6jhb03YKuYULtvA05gtnj-rTsom3L2Pe5T_5BlTPiXMbg0bry_ofgzWMFu2HGUW-jmyHe61-rKwBbABNDShHtb4RRvbeHXuyhiz303h5635b6S2Ncflh8qcZNTyqbRZlKFr_GqO_CLvqyridFbxeRhaBhHV3St5-bApQOSxcN5z8Bh6zXjQ
CitedBy_id crossref_primary_10_1128_IAI_00268_20
crossref_primary_10_3390_toxins11030167
crossref_primary_10_1016_j_vetpar_2023_109933
crossref_primary_10_1016_j_vaccine_2020_10_087
crossref_primary_10_1007_s10493_020_00584_1
crossref_primary_10_1016_j_dci_2016_11_013
crossref_primary_10_1111_imb_12193
crossref_primary_10_1038_srep37039
crossref_primary_10_3389_fcimb_2017_00429
crossref_primary_10_1016_j_fsi_2024_109799
Cites_doi 10.1016/j.pt.2005.02.004
10.1186/1471-2164-11-531
10.3389/fcimb.2014.00116
10.1016/j.dci.2009.12.005
10.1016/S0959-440X(01)00266-4
10.1128/CMR.13.3.451-469.2000
10.1128/AAC.46.11.3585-3590.2002
10.1126/science.1171400
10.1016/j.ijppaw.2012.11.003
10.1016/j.vetpar.2008.07.023
10.1016/S1471-4906(03)00242-4
10.1016/j.compbiomed.2014.07.016
10.1051/vetres/2009020
10.1016/j.ijpara.2008.03.001
10.1016/j.chom.2009.01.005
10.1016/j.devcel.2011.10.015
10.1016/0959-440X(95)80105-7
10.1016/j.ibmb.2011.12.001
10.1016/0968-0004(94)90090-6
10.1073/pnas.1010575107
10.1016/j.devcel.2009.06.016
10.1016/j.vetpar.2006.01.035
10.1016/j.vetpar.2006.01.048
10.1016/j.ijpara.2007.05.011
10.1371/journal.ppat.1002023
10.1159/000358017
10.1128/IAI.05214-11
10.1016/j.meegid.2012.07.004
10.1038/nprot.2009.2
10.1007/s00018-008-8019-0
10.1021/cb800138w
10.2741/3435
10.1006/jmbi.1998.1643
10.1073/pnas.1413638111
10.3389/fcimb.2013.00026
ContentType Journal Article
Copyright Springer-Verlag Berlin Heidelberg 2015
COPYRIGHT 2015 Springer
Copyright_xml – notice: Springer-Verlag Berlin Heidelberg 2015
– notice: COPYRIGHT 2015 Springer
DBID FBQ
AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
7S9
L.6
DOI 10.1007/s00436-015-4365-7
DatabaseName AGRIS
CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
AGRICOLA
AGRICOLA - Academic
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
AGRICOLA
AGRICOLA - Academic
DatabaseTitleList
AGRICOLA


MEDLINE - Academic

MEDLINE
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
– sequence: 3
  dbid: FBQ
  name: AGRIS
  url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN
  sourceTypes: Publisher
DeliveryMethod fulltext_linktorsrc
Discipline Zoology
EISSN 1432-1955
EndPage 1802
ExternalDocumentID A432550013
25690462
10_1007_s00436_015_4365_7
US201500169023
Genre Research Support, Non-U.S. Gov't
Journal Article
GroupedDBID ---
-4W
-56
-5G
-BR
-EM
-Y2
-~C
-~X
.55
.86
.VR
06C
06D
0R~
0VY
123
199
1N0
1SB
2.D
203
28-
29O
29~
2J2
2JN
2JY
2KG
2KM
2LR
2P1
2VQ
2~H
30V
3SX
4.4
406
408
409
40D
40E
53G
5QI
5VS
67N
67Z
6NX
78A
8TC
8UJ
95-
95.
95~
96X
AAAVM
AABHQ
AABYN
AAFGU
AAHNG
AAIAL
AAJKR
AANXM
AANZL
AARHV
AARTL
AATNV
AATVU
AAUYE
AAWCG
AAYFA
AAYIU
AAYQN
AAYTO
ABBBX
ABBXA
ABDZT
ABECU
ABELW
ABFGW
ABFTV
ABHLI
ABHQN
ABJNI
ABJOX
ABKAS
ABKCH
ABKTR
ABMNI
ABMQK
ABNWP
ABPLI
ABPTK
ABQBU
ABSXP
ABTEG
ABTHY
ABTKH
ABTMW
ABULA
ABWNU
ABXPI
ACBMV
ACBRV
ACBXY
ACBYP
ACGFS
ACHSB
ACHXU
ACIGE
ACIPQ
ACKNC
ACMDZ
ACMLO
ACOKC
ACOMO
ACPRK
ACTTH
ACVWB
ACWMK
ADHHG
ADHIR
ADIMF
ADINQ
ADKNI
ADKPE
ADMDM
ADOAH
ADOXG
ADRFC
ADTPH
ADURQ
ADYFF
ADYPR
ADZKW
AEBTG
AEEQQ
AEFIE
AEFTE
AEGAL
AEGNC
AEJHL
AEJRE
AEKMD
AENEX
AEOHA
AEPYU
AEQTP
AESKC
AESTI
AETLH
AEVLU
AEVTX
AEXYK
AFEXP
AFGCZ
AFLOW
AFNRJ
AFQWF
AFWTZ
AFZKB
AGAYW
AGDGC
AGGBP
AGGDS
AGJBK
AGMZJ
AGQMX
AGWIL
AGWZB
AGYKE
AHAVH
AHBYD
AHKAY
AHSBF
AHYZX
AIAKS
AIIXL
AILAN
AIMYW
AITGF
AJBLW
AJDOV
AJRNO
AJZVZ
AKMHD
AKQUC
ALMA_UNASSIGNED_HOLDINGS
ALWAN
AMKLP
AMXSW
AMYLF
AMYQR
AOCGG
AOSHJ
ARMRJ
ASPBG
AVWKF
AXYYD
AZFZN
B-.
BA0
BBWZM
BDATZ
BGNMA
CAG
COF
CS3
CSCUP
DDRTE
DL5
DNIVK
DPUIP
DU5
EBD
EBLON
EBS
ECGQY
EIOEI
EJD
EMOBN
EN4
EPAXT
ESBYG
F5P
FBQ
FEDTE
FERAY
FFXSO
FIGPU
FINBP
FNLPD
FRRFC
FSGXE
FWDCC
G-Y
G-Z
GGCAI
GGRSB
GJIRD
GNWQR
GQ6
GQ7
GQ8
GXS
HF~
HG5
HG6
HMJXF
HQYDN
HRMNR
HVGLF
HZ~
I09
IAO
IFM
IHE
IJ-
IKXTQ
INH
INR
ITM
IWAJR
IXC
IZIGR
IZQ
I~X
I~Z
J-C
J0Z
JBSCW
JCJTX
JZLTJ
KDC
KOV
KOW
KPH
L7B
LAS
LLZTM
M4Y
MA-
N2Q
NB0
NDZJH
NPVJJ
NQJWS
NU0
O9-
O93
O9G
O9I
O9J
OAM
OHT
P19
P2P
PF0
PT4
PT5
QOK
QOR
QOS
R89
R9I
RHV
RIG
RNI
RNS
ROL
RPX
RRX
RSV
RZK
S16
S1Z
S26
S27
S28
S3A
S3B
SAP
SBL
SBY
SCLPG
SDH
SDM
SHX
SISQX
SJYHP
SNE
SNPRN
SNX
SOHCF
SOJ
SPISZ
SRMVM
SSLCW
SSXJD
STPWE
SV3
SZN
T13
T16
TSG
TSK
TSV
TUC
U2A
U9L
UG4
UNUBA
UOJIU
UTJUX
UZXMN
VC2
VFIZW
W23
W48
WJK
WK6
WK8
X7M
YLTOR
Z45
Z7U
Z7V
Z7W
Z82
Z83
Z87
Z8O
Z8P
Z8Q
Z8V
Z8W
Z91
ZMTXR
ZOVNA
ZXP
~EX
~KM
AACDK
AAHBH
AAJBT
AAJSJ
AASML
AAYZH
ABAKF
ABQSL
ACAOD
ACPIV
ACULB
ACZOJ
AEFQL
AEMSY
AFBBN
AGQEE
AGRTI
AIGIU
BSONS
C6C
H13
IHR
AAPKM
AAYXX
ABBRH
ABDBE
ABEEZ
ABFSG
ACSTC
ADHKG
ADXHL
AEZWR
AFDZB
AFGXO
AFHIU
AFOHR
AGQPQ
AHPBZ
AHWEU
AIXLP
ATHPR
AYFIA
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
AEIIB
7X8
7S9
L.6
ID FETCH-LOGICAL-c604t-a6aa8cd93f75aed1b46743174564b398ca44247b4c8d63ff511feaff2b7eb7433
IEDL.DBID U2A
ISSN 0932-0113
1432-1955
IngestDate Fri Jul 11 13:50:09 EDT 2025
Fri Jul 11 10:11:56 EDT 2025
Tue Jun 17 21:19:40 EDT 2025
Tue Jun 10 20:30:47 EDT 2025
Thu Apr 03 06:57:54 EDT 2025
Tue Jul 01 03:57:42 EDT 2025
Thu Apr 24 23:08:08 EDT 2025
Fri Feb 21 02:27:02 EST 2025
Wed Dec 27 19:17:11 EST 2023
IsPeerReviewed true
IsScholarly true
Issue 5
Keywords Parasite
Leucine-rich repeat
Tick
Recombinant
Language English
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c604t-a6aa8cd93f75aed1b46743174564b398ca44247b4c8d63ff511feaff2b7eb7433
Notes http://dx.doi.org/10.1007/s00436-015-4365-7
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
PMID 25690462
PQID 1673371980
PQPubID 23479
PageCount 10
ParticipantIDs proquest_miscellaneous_1686703837
proquest_miscellaneous_1673371980
gale_infotracmisc_A432550013
gale_infotracacademiconefile_A432550013
pubmed_primary_25690462
crossref_primary_10_1007_s00436_015_4365_7
crossref_citationtrail_10_1007_s00436_015_4365_7
springer_journals_10_1007_s00436_015_4365_7
fao_agris_US201500169023
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 2015-05-01
PublicationDateYYYYMMDD 2015-05-01
PublicationDate_xml – month: 05
  year: 2015
  text: 2015-05-01
  day: 01
PublicationDecade 2010
PublicationPlace Berlin/Heidelberg
PublicationPlace_xml – name: Berlin/Heidelberg
– name: Germany
PublicationSubtitle Founded as Zeitschrift für Parasitenkunde
PublicationTitle Parasitology research (1987)
PublicationTitleAbbrev Parasitol Res
PublicationTitleAlternate Parasitol Res
PublicationYear 2015
Publisher Springer-Verlag
Springer Berlin Heidelberg
Springer
Publisher_xml – name: Springer-Verlag
– name: Springer Berlin Heidelberg
– name: Springer
References Bella, Hindle, McEwan, Lovell (CR4) 2008; 65
Bej, Sahoo, Swain, Basu, Jayasankar, Samanta (CR2) 2014; 53
Lutz (CR20) 2008; 3
Hunfeld, Hildebrandt, Gray (CR13) 2008; 38
Kelley, Sternberg (CR16) 2009; 4
Kobe, Deisenhofer (CR17) 1994; 19
Bell, Mullen, Leifer, Mazzoni, Davies, Segal (CR3) 2003; 24
Uilenberg (CR32) 2006; 138
Kobe, Deisenhofer (CR18) 1995; 5
Cirimotich, Dong, Garver, Sim, Dimopoulos (CR6) 2010; 34
Kajava (CR15) 1998; 277
Baxter, Steinert, Chelliah, Volohonsky, Levashina, Deisenhofer (CR1) 2010; 107
Umemiya-Shirafuji, Tanaka, Boldbaatar, Tanaka, Fujisaki (CR33) 2012; 42
Kagermeier-Schenk, Wehner, Ozhan-Kizil, Yamamoto, Li, Kirchner, Hoffmann, Stern, Kikuchi, Schambony, Weidinger (CR14) 2011; 21
MacDonald, Tamai, He (CR21) 2009; 17
Povelones, Waterhouse, Kafatos, Christophides (CR25) 2009; 324
Schmidt, Geilenkeuser, Sireis, Seifried, Hourfar (CR28) 2014; 41
Hill, Wikel (CR11) 2005; 21
Fraiture, Baxter, Steinert, Chelliah, Frolet, Quispe-Tintaya, Hoffmann, Blandin, Levashina (CR8) 2009; 5
Smith, Pal (CR30) 2014; 4
Florin-Christensen, Schnittger (CR7) 2009; 14
Fujisaki (CR9) 1978; 18
Kobe, Kajava (CR19) 2001; 11
Vial, Gorenflot (CR34) 2006; 138
CR27
Hajdušek, Síma, Ayllón, Jalovecká, Perner, de la Fuente, Kopáček (CR10) 2013; 3
Homer, Aguilar-Delfin, Telford, Krause, Persing (CR12) 2000; 13
Povelones, Upton, Sala, Christophides (CR26) 2011; 7
Matsuu, Yamasaki, Xuan, Ikadai, Hikasa (CR22) 2008; 157
Yabsley, Shock (CR36) 2013; 2
Pagel Van Zee, Geraci, Guerrero, Wikel, Stuart, Nene, Hill (CR24) 2007; 37
Schnittger, Rodriguez, Florin-Christensen, Morrison (CR29) 2012; 12
Stark, Liu, Deber (CR31) 2002; 46
Waterhouse, Povelones, Christophides (CR35) 2010; 11
Miyata, Harakuni, Tsuboi, Sattabongkot, Ikehara, Tachibana, Torii, Matsuzaki, Arakawa (CR23) 2011; 79
Chauvin, Moreau, Bonnet, Plantard, Malandrin (CR5) 2009; 40
JK Bell (4365_CR3) 2003; 24
M Stark (4365_CR31) 2002; 46
HJ Vial (4365_CR34) 2006; 138
J Pagel Van Zee (4365_CR24) 2007; 37
M Schmidt (4365_CR28) 2014; 41
G Uilenberg (4365_CR32) 2006; 138
BT MacDonald (4365_CR21) 2009; 17
RM Waterhouse (4365_CR35) 2010; 11
4365_CR27
B Kobe (4365_CR17) 1994; 19
K Fujisaki (4365_CR9) 1978; 18
LA Kelley (4365_CR16) 2009; 4
MJ Homer (4365_CR12) 2000; 13
A Matsuu (4365_CR22) 2008; 157
T Miyata (4365_CR23) 2011; 79
R Umemiya-Shirafuji (4365_CR33) 2012; 42
B Kagermeier-Schenk (4365_CR14) 2011; 21
MJ Yabsley (4365_CR36) 2013; 2
A Bej (4365_CR2) 2014; 53
M Povelones (4365_CR26) 2011; 7
AV Kajava (4365_CR15) 1998; 277
CM Cirimotich (4365_CR6) 2010; 34
O Hajdušek (4365_CR10) 2013; 3
J Bella (4365_CR4) 2008; 65
AA Smith (4365_CR30) 2014; 4
M Florin-Christensen (4365_CR7) 2009; 14
CS Lutz (4365_CR20) 2008; 3
B Kobe (4365_CR19) 2001; 11
B Kobe (4365_CR18) 1995; 5
A Chauvin (4365_CR5) 2009; 40
M Fraiture (4365_CR8) 2009; 5
L Schnittger (4365_CR29) 2012; 12
KP Hunfeld (4365_CR13) 2008; 38
RH Baxter (4365_CR1) 2010; 107
CA Hill (4365_CR11) 2005; 21
M Povelones (4365_CR25) 2009; 324
21533217 - PLoS Pathog. 2011 Apr;7(4):e1002023
18771856 - Vet Parasitol. 2008 Oct 20;157(1-2):1-8
18440005 - Int J Parasitol. 2008 Sep;38(11):1219-37
11751054 - Curr Opin Struct Biol. 2001 Dec;11(6):725-32
19247286 - Nat Protoc. 2009;4(3):363-71
12384369 - Antimicrob Agents Chemother. 2002 Nov;46(11):3585-90
77478 - Natl Inst Anim Health Q (Tokyo). 1978 Spring;18(1):27-38
22871652 - Infect Genet Evol. 2012 Dec;12(8):1788-809
19264986 - Science. 2009 Apr 10;324(5924):258-61
25150822 - Comput Biol Med. 2014 Oct;53:164-70
19273257 - Front Biosci (Landmark Ed). 2009 Jan 01;14:3064-73
10885987 - Clin Microbiol Rev. 2000 Jul;13(3):451-69
16504402 - Vet Parasitol. 2006 May 31;138(1-2):147-60
19286136 - Cell Host Microbe. 2009 Mar 19;5(3):273-84
21807905 - Infect Immun. 2011 Oct;79(10):4260-75
23875177 - Front Cell Infect Microbiol. 2013 Jul 16;3:26
25427795 - Proc Natl Acad Sci U S A. 2014 Dec 16;111(50):17875-80
7583641 - Curr Opin Struct Biol. 1995 Jun;5(3):409-16
22193391 - Insect Biochem Mol Biol. 2012 Mar;42(3):164-73
18408889 - Cell Mol Life Sci. 2008 Aug;65(15):2307-33
24659943 - Transfus Med Hemother. 2014 Feb;41(1):10-7
25202684 - Front Cell Infect Microbiol. 2014 Aug 22;4:116
14552836 - Trends Immunol. 2003 Oct;24(10):528-33
20826443 - Proc Natl Acad Sci U S A. 2010 Sep 28;107(39):16817-22
9533877 - J Mol Biol. 1998 Apr 3;277(3):519-27
19619488 - Dev Cell. 2009 Jul;17(1):9-26
24533312 - Int J Parasitol Parasites Wildl. 2012 Nov 22;2:18-31
16513280 - Vet Parasitol. 2006 May 31;138(1-2):3-10
19379662 - Vet Res. 2009 Mar-Apr;40(2):37
22100263 - Dev Cell. 2011 Dec 13;21(6):1129-43
18817380 - ACS Chem Biol. 2008 Oct 17;3(10):609-17
7817399 - Trends Biochem Sci. 1994 Oct;19(10):415-21
15780833 - Trends Parasitol. 2005 Apr;21(4):151-3
20920294 - BMC Genomics. 2010 Sep 30;11:531
17624352 - Int J Parasitol. 2007 Oct;37(12):1297-305
20026176 - Dev Comp Immunol. 2010 Apr;34(4):387-95
References_xml – volume: 21
  start-page: 151
  year: 2005
  end-page: 153
  ident: CR11
  article-title: The Genome Project: an opportunity for advancing tick research
  publication-title: Trends Parasitol
  doi: 10.1016/j.pt.2005.02.004
– volume: 3
  start-page: 26
  year: 2013
  ident: CR10
  article-title: Interaction of the tick immune system with transmitted pathogens
  publication-title: Front Cell Infect Microbiol
– volume: 11
  start-page: 531
  year: 2010
  ident: CR35
  article-title: Sequence-structure-function relations of the mosquito leucine-rich repeat immune proteins
  publication-title: BMC Genomics
  doi: 10.1186/1471-2164-11-531
– volume: 4
  start-page: 116
  year: 2014
  ident: CR30
  article-title: Immunity-related genes in —perspectives from genome information
  publication-title: Front Cell Infect Microbiol
  doi: 10.3389/fcimb.2014.00116
– volume: 34
  start-page: 387
  year: 2010
  end-page: 395
  ident: CR6
  article-title: Mosquito immune defenses against infection
  publication-title: Dev Comp Immunol
  doi: 10.1016/j.dci.2009.12.005
– volume: 11
  start-page: 725
  year: 2001
  end-page: 732
  ident: CR19
  article-title: The leucine-rich repeat as a protein recognition motif
  publication-title: Curr Opin Struct Biol
  doi: 10.1016/S0959-440X(01)00266-4
– volume: 13
  start-page: 451
  year: 2000
  end-page: 469
  ident: CR12
  article-title: Babesiosis
  publication-title: Clin Microbiol
  doi: 10.1128/CMR.13.3.451-469.2000
– volume: 46
  start-page: 3585
  year: 2002
  end-page: 3590
  ident: CR31
  article-title: Cationic hydrophobic peptides with antimicrobial activity
  publication-title: Antimicrob Agents Chemother
  doi: 10.1128/AAC.46.11.3585-3590.2002
– volume: 324
  start-page: 258
  year: 2009
  end-page: 261
  ident: CR25
  article-title: Leucine-rich repeat protein complex activates mosquito complement in defense against parasites
  publication-title: Science
  doi: 10.1126/science.1171400
– volume: 2
  start-page: 18
  year: 2013
  end-page: 31
  ident: CR36
  article-title: Natural history of zoonotic : role of wildlife reservoirs
  publication-title: Int J Parasitol Parasites Wildl
  doi: 10.1016/j.ijppaw.2012.11.003
– volume: 157
  start-page: 1
  year: 2008
  end-page: 8
  ident: CR22
  article-title: In vitro evaluation of the growth inhibitory activities of 15 drugs against (Aomori strain)
  publication-title: Vet Parasitol
  doi: 10.1016/j.vetpar.2008.07.023
– volume: 24
  start-page: 528
  year: 2003
  end-page: 533
  ident: CR3
  article-title: Leucine-rich repeats and pathogen recognition in Toll-like receptors
  publication-title: Trends Immunol
  doi: 10.1016/S1471-4906(03)00242-4
– volume: 53
  start-page: 164
  year: 2014
  end-page: 170
  ident: CR2
  article-title: LRRsearch: An asynchronous server-based application for the prediction of leucine-rich repeat motifs and an integrative database of NOD-like receptors
  publication-title: Comput Biol Med
  doi: 10.1016/j.compbiomed.2014.07.016
– volume: 40
  start-page: 37
  year: 2009
  ident: CR5
  article-title: and its hosts: adaptation to long-lasting interactions as a way to achieve efficient transmission
  publication-title: Vet Res
  doi: 10.1051/vetres/2009020
– volume: 38
  start-page: 1219
  year: 2008
  end-page: 1237
  ident: CR13
  article-title: Babesiosis: recent insights into an ancient disease
  publication-title: Int J Parasitol
  doi: 10.1016/j.ijpara.2008.03.001
– ident: CR27
– volume: 5
  start-page: 273
  year: 2009
  end-page: 284
  ident: CR8
  article-title: Two mosquito LRR domain-containing proteins function as complement control factors in the TEP1-mediated killing of
  publication-title: Cell Host Microbe
  doi: 10.1016/j.chom.2009.01.005
– volume: 21
  start-page: 1129
  year: 2011
  end-page: 1143
  ident: CR14
  article-title: Waif1/5 T4 inhibits Wnt/β-catenin signaling and activates noncanonical Wnt pathways by modifying LRP6 subcellular localization
  publication-title: Dev Cell
  doi: 10.1016/j.devcel.2011.10.015
– volume: 5
  start-page: 409
  year: 1995
  end-page: 416
  ident: CR18
  article-title: Proteins with leucine-rich repeats
  publication-title: Curr Opin Struct Biol
  doi: 10.1016/0959-440X(95)80105-7
– volume: 18
  start-page: 27
  year: 1978
  end-page: 38
  ident: CR9
  article-title: Development of acquired resistance precipitating antibody in rabbits experimentally infested with females of (Ixodoidea: Ixodidae)
  publication-title: Natl Inst Anim Health Q (Tokyo)
– volume: 42
  start-page: 164
  year: 2012
  end-page: 173
  ident: CR33
  article-title: Akt is an essential player in regulating cell/organ growth at the adult stage in the hard tick
  publication-title: Insect Biochem Mol Biol
  doi: 10.1016/j.ibmb.2011.12.001
– volume: 19
  start-page: 415
  year: 1994
  end-page: 421
  ident: CR17
  article-title: The leucine-rich repeat: a versatile binding motif
  publication-title: Trends Biochem Sci
  doi: 10.1016/0968-0004(94)90090-6
– volume: 107
  start-page: 16817
  year: 2010
  end-page: 16822
  ident: CR1
  article-title: A heterodimeric complex of the LRR domain-containing proteins LRIM1 and APL1C regulates complement-like immunity in
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.1010575107
– volume: 17
  start-page: 9
  year: 2009
  end-page: 26
  ident: CR21
  article-title: Wnt/beta-catenin signaling: components, mechanisms, and diseases
  publication-title: Dev Cell
  doi: 10.1016/j.devcel.2009.06.016
– volume: 138
  start-page: 3
  year: 2006
  end-page: 10
  ident: CR32
  article-title: -a historical overview
  publication-title: Vet Parasitol
  doi: 10.1016/j.vetpar.2006.01.035
– volume: 138
  start-page: 147
  year: 2006
  end-page: 160
  ident: CR34
  article-title: Chemotherapy against babesiosis
  publication-title: Vet Parasitol
  doi: 10.1016/j.vetpar.2006.01.048
– volume: 37
  start-page: 1297
  year: 2007
  end-page: 1305
  ident: CR24
  article-title: Tick genomics: the Ixodes genome project and beyond
  publication-title: Int J Parasitol
  doi: 10.1016/j.ijpara.2007.05.011
– volume: 7
  start-page: e1002023
  year: 2011
  ident: CR26
  article-title: Structure-function analysis of the LRIM1/APL1C complex and its interaction with complement C3-like protein TEP1
  publication-title: PLoS Pathog
  doi: 10.1371/journal.ppat.1002023
– volume: 41
  start-page: 10
  year: 2014
  end-page: 17
  ident: CR28
  article-title: Emerging pathogens—how safe is blood?
  publication-title: Transfus Med Hemother
  doi: 10.1159/000358017
– volume: 79
  start-page: 4260
  year: 2011
  end-page: 4275
  ident: CR23
  article-title: Tricomponent immunopotentiating system as a novel molecular design strategy for malaria vaccine development
  publication-title: Infect Immun
  doi: 10.1128/IAI.05214-11
– volume: 12
  start-page: 1788
  year: 2012
  end-page: 1809
  ident: CR29
  article-title: : a world emerging
  publication-title: Infect Genet Evol
  doi: 10.1016/j.meegid.2012.07.004
– volume: 4
  start-page: 363
  year: 2009
  end-page: 371
  ident: CR16
  article-title: Protein structure prediction on the Web: a case study using the Phyre server
  publication-title: Nat Protoc
  doi: 10.1038/nprot.2009.2
– volume: 65
  start-page: 2307
  year: 2008
  end-page: 2333
  ident: CR4
  article-title: The leucine-rich repeat structure
  publication-title: Cell Mol Life Sci
  doi: 10.1007/s00018-008-8019-0
– volume: 3
  start-page: 609
  year: 2008
  end-page: 617
  ident: CR20
  article-title: Alternative polyadenylation: a twist on mRNA 3' end formation
  publication-title: ACS Chem Biol
  doi: 10.1021/cb800138w
– volume: 14
  start-page: 3064
  year: 2009
  end-page: 3073
  ident: CR7
  article-title: Piroplasmids and ticks: a long-lasting intimate relationship
  publication-title: Front Biosci
  doi: 10.2741/3435
– volume: 277
  start-page: 519
  year: 1998
  end-page: 527
  ident: CR15
  article-title: Structural diversity of leucine-rich repeat proteins
  publication-title: J Mol Biol
  doi: 10.1006/jmbi.1998.1643
– volume: 53
  start-page: 164
  year: 2014
  ident: 4365_CR2
  publication-title: Comput Biol Med
  doi: 10.1016/j.compbiomed.2014.07.016
– volume: 5
  start-page: 273
  year: 2009
  ident: 4365_CR8
  publication-title: Cell Host Microbe
  doi: 10.1016/j.chom.2009.01.005
– volume: 21
  start-page: 151
  year: 2005
  ident: 4365_CR11
  publication-title: Trends Parasitol
  doi: 10.1016/j.pt.2005.02.004
– volume: 14
  start-page: 3064
  year: 2009
  ident: 4365_CR7
  publication-title: Front Biosci
  doi: 10.2741/3435
– volume: 42
  start-page: 164
  year: 2012
  ident: 4365_CR33
  publication-title: Insect Biochem Mol Biol
  doi: 10.1016/j.ibmb.2011.12.001
– volume: 277
  start-page: 519
  year: 1998
  ident: 4365_CR15
  publication-title: J Mol Biol
  doi: 10.1006/jmbi.1998.1643
– ident: 4365_CR27
  doi: 10.1073/pnas.1413638111
– volume: 41
  start-page: 10
  year: 2014
  ident: 4365_CR28
  publication-title: Transfus Med Hemother
  doi: 10.1159/000358017
– volume: 157
  start-page: 1
  year: 2008
  ident: 4365_CR22
  publication-title: Vet Parasitol
  doi: 10.1016/j.vetpar.2008.07.023
– volume: 40
  start-page: 37
  year: 2009
  ident: 4365_CR5
  publication-title: Vet Res
  doi: 10.1051/vetres/2009020
– volume: 5
  start-page: 409
  year: 1995
  ident: 4365_CR18
  publication-title: Curr Opin Struct Biol
  doi: 10.1016/0959-440X(95)80105-7
– volume: 3
  start-page: 609
  year: 2008
  ident: 4365_CR20
  publication-title: ACS Chem Biol
  doi: 10.1021/cb800138w
– volume: 38
  start-page: 1219
  year: 2008
  ident: 4365_CR13
  publication-title: Int J Parasitol
  doi: 10.1016/j.ijpara.2008.03.001
– volume: 12
  start-page: 1788
  year: 2012
  ident: 4365_CR29
  publication-title: Infect Genet Evol
  doi: 10.1016/j.meegid.2012.07.004
– volume: 37
  start-page: 1297
  year: 2007
  ident: 4365_CR24
  publication-title: Int J Parasitol
  doi: 10.1016/j.ijpara.2007.05.011
– volume: 46
  start-page: 3585
  year: 2002
  ident: 4365_CR31
  publication-title: Antimicrob Agents Chemother
  doi: 10.1128/AAC.46.11.3585-3590.2002
– volume: 2
  start-page: 18
  year: 2013
  ident: 4365_CR36
  publication-title: Int J Parasitol Parasites Wildl
  doi: 10.1016/j.ijppaw.2012.11.003
– volume: 65
  start-page: 2307
  year: 2008
  ident: 4365_CR4
  publication-title: Cell Mol Life Sci
  doi: 10.1007/s00018-008-8019-0
– volume: 79
  start-page: 4260
  year: 2011
  ident: 4365_CR23
  publication-title: Infect Immun
  doi: 10.1128/IAI.05214-11
– volume: 21
  start-page: 1129
  year: 2011
  ident: 4365_CR14
  publication-title: Dev Cell
  doi: 10.1016/j.devcel.2011.10.015
– volume: 24
  start-page: 528
  year: 2003
  ident: 4365_CR3
  publication-title: Trends Immunol
  doi: 10.1016/S1471-4906(03)00242-4
– volume: 11
  start-page: 531
  year: 2010
  ident: 4365_CR35
  publication-title: BMC Genomics
  doi: 10.1186/1471-2164-11-531
– volume: 4
  start-page: 116
  year: 2014
  ident: 4365_CR30
  publication-title: Front Cell Infect Microbiol
  doi: 10.3389/fcimb.2014.00116
– volume: 138
  start-page: 147
  year: 2006
  ident: 4365_CR34
  publication-title: Vet Parasitol
  doi: 10.1016/j.vetpar.2006.01.048
– volume: 7
  start-page: e1002023
  year: 2011
  ident: 4365_CR26
  publication-title: PLoS Pathog
  doi: 10.1371/journal.ppat.1002023
– volume: 107
  start-page: 16817
  year: 2010
  ident: 4365_CR1
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.1010575107
– volume: 4
  start-page: 363
  year: 2009
  ident: 4365_CR16
  publication-title: Nat Protoc
  doi: 10.1038/nprot.2009.2
– volume: 18
  start-page: 27
  year: 1978
  ident: 4365_CR9
  publication-title: Natl Inst Anim Health Q (Tokyo)
– volume: 17
  start-page: 9
  year: 2009
  ident: 4365_CR21
  publication-title: Dev Cell
  doi: 10.1016/j.devcel.2009.06.016
– volume: 34
  start-page: 387
  year: 2010
  ident: 4365_CR6
  publication-title: Dev Comp Immunol
  doi: 10.1016/j.dci.2009.12.005
– volume: 19
  start-page: 415
  year: 1994
  ident: 4365_CR17
  publication-title: Trends Biochem Sci
  doi: 10.1016/0968-0004(94)90090-6
– volume: 11
  start-page: 725
  year: 2001
  ident: 4365_CR19
  publication-title: Curr Opin Struct Biol
  doi: 10.1016/S0959-440X(01)00266-4
– volume: 13
  start-page: 451
  year: 2000
  ident: 4365_CR12
  publication-title: Clin Microbiol
  doi: 10.1128/CMR.13.3.451-469.2000
– volume: 138
  start-page: 3
  year: 2006
  ident: 4365_CR32
  publication-title: Vet Parasitol
  doi: 10.1016/j.vetpar.2006.01.035
– volume: 3
  start-page: 26
  year: 2013
  ident: 4365_CR10
  publication-title: Front Cell Infect Microbiol
  doi: 10.3389/fcimb.2013.00026
– volume: 324
  start-page: 258
  year: 2009
  ident: 4365_CR25
  publication-title: Science
  doi: 10.1126/science.1171400
– reference: 16513280 - Vet Parasitol. 2006 May 31;138(1-2):3-10
– reference: 22100263 - Dev Cell. 2011 Dec 13;21(6):1129-43
– reference: 19286136 - Cell Host Microbe. 2009 Mar 19;5(3):273-84
– reference: 17624352 - Int J Parasitol. 2007 Oct;37(12):1297-305
– reference: 25427795 - Proc Natl Acad Sci U S A. 2014 Dec 16;111(50):17875-80
– reference: 11751054 - Curr Opin Struct Biol. 2001 Dec;11(6):725-32
– reference: 10885987 - Clin Microbiol Rev. 2000 Jul;13(3):451-69
– reference: 19273257 - Front Biosci (Landmark Ed). 2009 Jan 01;14:3064-73
– reference: 18440005 - Int J Parasitol. 2008 Sep;38(11):1219-37
– reference: 22871652 - Infect Genet Evol. 2012 Dec;12(8):1788-809
– reference: 77478 - Natl Inst Anim Health Q (Tokyo). 1978 Spring;18(1):27-38
– reference: 18408889 - Cell Mol Life Sci. 2008 Aug;65(15):2307-33
– reference: 20920294 - BMC Genomics. 2010 Sep 30;11:531
– reference: 25202684 - Front Cell Infect Microbiol. 2014 Aug 22;4:116
– reference: 22193391 - Insect Biochem Mol Biol. 2012 Mar;42(3):164-73
– reference: 14552836 - Trends Immunol. 2003 Oct;24(10):528-33
– reference: 15780833 - Trends Parasitol. 2005 Apr;21(4):151-3
– reference: 19247286 - Nat Protoc. 2009;4(3):363-71
– reference: 21533217 - PLoS Pathog. 2011 Apr;7(4):e1002023
– reference: 19379662 - Vet Res. 2009 Mar-Apr;40(2):37
– reference: 19264986 - Science. 2009 Apr 10;324(5924):258-61
– reference: 7583641 - Curr Opin Struct Biol. 1995 Jun;5(3):409-16
– reference: 23875177 - Front Cell Infect Microbiol. 2013 Jul 16;3:26
– reference: 24533312 - Int J Parasitol Parasites Wildl. 2012 Nov 22;2:18-31
– reference: 20826443 - Proc Natl Acad Sci U S A. 2010 Sep 28;107(39):16817-22
– reference: 16504402 - Vet Parasitol. 2006 May 31;138(1-2):147-60
– reference: 12384369 - Antimicrob Agents Chemother. 2002 Nov;46(11):3585-90
– reference: 20026176 - Dev Comp Immunol. 2010 Apr;34(4):387-95
– reference: 7817399 - Trends Biochem Sci. 1994 Oct;19(10):415-21
– reference: 9533877 - J Mol Biol. 1998 Apr 3;277(3):519-27
– reference: 18771856 - Vet Parasitol. 2008 Oct 20;157(1-2):1-8
– reference: 24659943 - Transfus Med Hemother. 2014 Feb;41(1):10-7
– reference: 19619488 - Dev Cell. 2009 Jul;17(1):9-26
– reference: 21807905 - Infect Immun. 2011 Oct;79(10):4260-75
– reference: 25150822 - Comput Biol Med. 2014 Oct;53:164-70
– reference: 18817380 - ACS Chem Biol. 2008 Oct 17;3(10):609-17
SSID ssj0017644
Score 2.1476989
Snippet Haemaphysalis longicornis is a tick known for transmitting Babesia parasites, including Babesia gibsoni, in East Asian countries. The vector tick must have...
Haemaphysalis longicornis is a tick known for transmitting Babesia parasites, including Babesia gibsoni , in East Asian countries. The vector tick must have...
SourceID proquest
gale
pubmed
crossref
springer
fao
SourceType Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 1793
SubjectTerms Animals
Babesia
Babesia - genetics
Babesia - physiology
Babesia gibsoni
babesiosis
Biomedical and Life Sciences
Biomedicine
blood
Digestive System
drugs
gene expression regulation
Gene Expression Regulation - physiology
growth retardation
Haemaphysalis longicornis
Hard ticks
Health aspects
hematophagy
Host-Parasite Interactions
Host-parasite relationships
Immunology
innate immunity
Ixodidae - parasitology
Leucine
Medical Microbiology
Merozoites
messenger RNA
Microbiology
midgut
Observations
Original Paper
proteins
Proteins - metabolism
Salivary Glands
ticks
Title Identification of the Babesia-responsive leucine-rich repeat domain-containing protein from the hard tick Haemaphysalis longicornis
URI https://link.springer.com/article/10.1007/s00436-015-4365-7
https://www.ncbi.nlm.nih.gov/pubmed/25690462
https://www.proquest.com/docview/1673371980
https://www.proquest.com/docview/1686703837
Volume 114
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1Lj9MwELborpC4IJbXBnYrIyEhgSw1sWMnx7baUoHYC1RauFiOYy8rusmqafkD_HFmnIcoj5U45ZDJc-yZsWe-bwh56ZWLuRCclXlpmFDSMXAKJUN_YcoiTU1AeH84l8uVeHeRXnQ47qavdu9TksFSD2C3wJYOS9-UCSzNUiNymOLSHQbxKpkOqQMlQwdXWKljzUHM-1Tm326x54xG3tR_GuZfPNNvqdLggRYPyP0udKTTVtdH5I6rHpK7X-qwMf6I_Ggxt77bhKO1pxDc0ZlB6n_DNl0x7HdH126H6XQGJvAr3bgbMMe0rK_NVcWwcr3tGUEDg8NVRRGAEu6E-CwKz_5Gl8ZdI891g-yJdF1XYD4R39U8JqvF2af5knUtFpiVE7FlRhqT2TLnXqXGlXGBzUcgpECSmYLnmTVCJEIVwmal5N5DeOad8T4plCtAkj8hB1VduWNCrXTOC-5zU0CUYJPCGOl8mqeT2Ge5tRGZ9P9a245_HNtgrPXAnBzUo0E9GtWjVUReD5fctOQbtwkfgwK1uQTjqFcfE9zKQaoZCEoi8gq1qnHOwiOt6aAH8OLIfqWngsPKCqPhiJzsScJcs3unX_TjQuMpLFCrXL1rdCwV5yrOs8ltMpkEA5txeNen7aAaPgsizxxxwhF5048y3VmT5t_f_Oy_pJ-Te_hX2nLNE3Kw3ezcKYRU22JMDqeL2ewcj28_vz8bk9FczsdhYv0EpCAZww
linkProvider Springer Nature
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1Lb9QwELZoEYIL4t2UAkZCQgJZ2qwdOzmWFdUCbS90pYqLNXbsUrFNqn30D_DHmXGyK7ZAJc6ZvDz2zGfPzDeMvYkm5FIpKeqqBqGMDgKdQi3IX0DtigJShffRsR5P1OfT4rQni6ZamGvx-0T2KWnPWwhFCVlmi91WuFGm7L2RHq0DBkanvq24P6dMg1yuAph_e8SGC9qK0P5pjn_zR9cCpMnvHDxg93vAyPc7DT9kt0LziN351qbj8MfsZ1dpG_ujN95GjpCOfwAi_Acx61NgrwKfhiUF0QUavu98Fi7RCPO6vYDzRlC-etcpgifehvOGU9lJehJVZXF89w8-hnBB7NZz4kzk07ZBo0lVXfMnbHLw8WQ0Fn1jBeH1QC0EaIDS15WMpoBQ545ajiCQIGoZJ6vSg1JDZZzyZa1ljAjKYoAYh84Eh5LyKdtu2ibsMO51CFHJWIFDbOCHDkCHWFTFII9l5X3GBquxtr5nHafmF1O75ktO6rGoHkvqsSZj79a3XHaUGzcJ76ACLZyhSbSTr0M6wCGCGYQiGXtLWrW0UvGVHvqCA_xw4ryy-0rifoowcMb2NiRxhfmNy69X88LSJUpLa0K7nNtcGykNTsfBTTKlRrNaSvzWZ92kWv8W4s2KqoMz9n41y2xvQ-b__ufd_5J-xe6OT44O7eGn4y_P2T0aoS5hc49tL2bL8AJB1cK9TMvpF-uzFKg
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3db9MwELdYJxAvfMMCA4yEhATy1tSOnTwWWCkMJiSotPFiHMeGaV1SNSkPvPKPc5cv0QGTEM-5JLZzufvZd_c7Qh575UIuBGdZkhkmlHQMnELG0F-YLI0iU1d4vzuQ05l4cxgdtn1Oyy7bvQtJNjUNyNKUV7uLzO_2hW81czpsgyMmME1LbZBNgdR2A7I5fnW0v9cHEpSs-7nCvh0zEELeBTb_9JA117ThTfG7mf7FT50JnNb-aHKVfO5m0qShnOysqnTHfj9D8vgfU71GrrRYlY4b5bpOLrj8Brn4qahP4m-SH02Rr29P_WjhKaBJ-txgrwHDlm327TdH526F8XsGNvcrXboF2H-aFafmOGc4mKZJBa0pI45zihUv9ZOwIIzCu0_o1LhTJNYuka6Rzosc7DUWlJW3yGyy9_HFlLU9HZiVQ1ExI42JbZZwryLjsjDFbieAYZDVJuVJbI0QI6FSYeNMcu8BD3pnvB-lyqUgyW-TQV7kbotQK53zgvvEpABL7Cg1RjofJdEw9HFibUCG3efUtiU8x74bc91TNddrq2FtNa6tVgF52t-yaNg-zhPeAh3R5gtYYz37MMKzI-S2ARQUkCeoOBqNBLzSmrbWAQaOdFt6LDhs5RB-B2R7TRJ-brt2-VGnehovYUZc7opVqUOpOFdhEg_Pk4klWPSYw1jvNHrbTwugboKFyQF51umgbs1X-fc53_0n6Yfk0vuXE_329cH-PXIZF6hJFd0mg2q5cvcBzlXpg_aX_Qkmij5w
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Identification+of+the+Babesia-responsive+leucine-rich+repeat+domain-containing+protein+from+the+hard+tick+Haemaphysalis+longicornis&rft.jtitle=Parasitology+research+%281987%29&rft.au=Maeda%2C+Hiroki&rft.au=Kurisu%2C+Koshi&rft.au=Miyata%2C+Takeshi&rft.au=Kusakisako%2C+Kodai&rft.date=2015-05-01&rft.pub=Springer&rft.issn=0932-0113&rft.volume=114&rft.issue=5&rft.spage=1793&rft_id=info:doi/10.1007%2Fs00436-015-4365-7&rft.externalDocID=A432550013
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0932-0113&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0932-0113&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0932-0113&client=summon