Characterization of Leptospiral Outer Membrane Lipoprotein LipL36: Downregulation Associated with Late-Log-Phase Growth and Mammalian Infection

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Published inInfection and Immunity Vol. 66; no. 4; pp. 1579 - 1587
Main Authors HAAKE, D. A, MARTINICH, C, SUMMERS, T. A, SHANG, E. S, PRUETZ, J. D, MCCOY, A. M, MAZEL, M. K, BOLIN, C. A
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.04.1998
Subjects
Amino Acid Sequence
Animals
Anti-Bacterial Agents - pharmacology
Antibodies, Bacterial - blood
Bacterial Outer Membrane Proteins - genetics
Bacteriology
Base Sequence
Biological and medical sciences
Cricetinae
Down-Regulation
Female
Fundamental and applied biological sciences. Psychology
Leptospira - chemistry
Leptospira - growth & development
Leptospira - immunology
Leptospirosis - metabolism
Male
Mesocricetus
Mice
Microbiology
Molecular and Cellular Pathogenesis
Molecular Sequence Data
Octoxynol - pharmacology
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
Peptides
Solubility
Membrane protein
Spirochaetales
Host agent relation
Lipoprotein
Gene expression
External membrane
Characterization
Gene
Leptospiraceae
Bacteria
Molecular cloning
Structural analysis
Leptospira
Online AccessGet full text

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AbstractList We report the cloning of the gene encoding a 36-kDa leptospiral outer membrane lipoprotein, designated LipL36. We obtained the N-terminal amino acid sequence of a staphylococcal V8 proteolytic-digest fragment in order to design an oligonucleotide probe. A Lambda-Zap II library containing EcoRI fragments of Leptospira kirschneri DNA was screened, and a 2.3-kb DNA fragment which contained the entire structural lipL36 gene was identified. Several lines of evidence indicate that LipL36 is lipid modified in a manner similar to that of LipL41, a leptospiral outer membrane lipoprotein we described in a previous study (E. S. Shang, T. A. Summers, and D. A. Haake, Infect. Immun. 64:2322-2330, 1996). The deduced amino acid sequence of LipL36 would constitute a 364-amino-acid polypeptide with a 20-amino-acid signal peptide, followed by an L-X-Y-C lipoprotein signal peptidase cleavage site. LipL36 is solubilized by Triton X-114 extraction of L. kirschneri; phase separation results in partitioning of LipL36 exclusively into the hydrophobic, detergent phase. LipL36 is intrinsically labeled during incubation of L. kirschneri in media containing [3H]palmitate. Processing of LipL36 is inhibited by globomycin, a selective inhibitor of lipoprotein signal peptidase. After processing, LipL36 is exported to the outer membrane along with LipL41 and lipopolysaccharide. Unlike LipL41, there appears to be differential expression of LipL36. In early-log-phase cultures, LipL36 is one of the most abundant L. kirschneri proteins. However, LipL36 levels drop considerably beginning in mid-log phase. LipL36 expression in vivo was evaluated by examining the humoral immune response to leptospiral antigens in the hamster model of leptospirosis. Hamsters surviving challenge with culture-adapted virulent L. kirschneri generate a strong antibody response to LipL36. In contrast, sera from hamsters surviving challenge with host-adapted L. kirschneri do not recognize LipL36. These findings suggest that LipL36 expression is downregulated during mammalian infection, providing a marker for studying the mechanisms by which pathogenic Leptospira species adapt to the host environment.
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ABSTRACT We report the cloning of the gene encoding a 36-kDa leptospiral outer membrane lipoprotein, designated LipL36. We obtained the N-terminal amino acid sequence of a staphylococcal V8 proteolytic-digest fragment in order to design an oligonucleotide probe. A Lambda-Zap II library containing Eco RI fragments of Leptospira kirschneri DNA was screened, and a 2.3-kb DNA fragment which contained the entire structural lipL36 gene was identified. Several lines of evidence indicate that LipL36 is lipid modified in a manner similar to that of LipL41, a leptospiral outer membrane lipoprotein we described in a previous study (E. S. Shang, T. A. Summers, and D. A. Haake, Infect. Immun. 64:2322–2330, 1996). The deduced amino acid sequence of LipL36 would constitute a 364-amino-acid polypeptide with a 20-amino-acid signal peptide, followed by an L-X-Y-C lipoprotein signal peptidase cleavage site. LipL36 is solubilized by Triton X-114 extraction of L. kirschneri ; phase separation results in partitioning of LipL36 exclusively into the hydrophobic, detergent phase. LipL36 is intrinsically labeled during incubation of L. kirschneri in media containing [ 3 H]palmitate. Processing of LipL36 is inhibited by globomycin, a selective inhibitor of lipoprotein signal peptidase. After processing, LipL36 is exported to the outer membrane along with LipL41 and lipopolysaccharide. Unlike LipL41, there appears to be differential expression of LipL36. In early-log-phase cultures, LipL36 is one of the most abundant L. kirschneri proteins. However, LipL36 levels drop considerably beginning in mid-log phase. LipL36 expression in vivo was evaluated by examining the humoral immune response to leptospiral antigens in the hamster model of leptospirosis. Hamsters surviving challenge with culture-adapted virulent L. kirschneri generate a strong antibody response to LipL36. In contrast, sera from hamsters surviving challenge with host-adapted L. kirschneri do not recognize LipL36. These findings suggest that LipL36 expression is downregulated during mammalian infection, providing a marker for studying the mechanisms by which pathogenic Leptospira species adapt to the host environment.
We report the cloning of the gene encoding a 36-kDa leptospiral outer membrane lipoprotein, designated LipL36. We obtained the N-terminal amino acid sequence of a staphylococcal V8 proteolytic-digest fragment in order to design an oligonucleotide probe. A Lambda-Zap II library containing EcoRI fragments of Leptospira kirschneri DNA was screened, and a 2.3-kb DNA fragment which contained the entire structural lipL36 gene was identified. Several lines of evidence indicate that LipL36 is lipid modified in a manner similar to that of LipL41, a leptospiral outer membrane lipoprotein we described in a previous study. The deduced amino acid sequence of LipL36 would constitute a 364-amino-acid polypeptide with a 20-amino-acid signal peptide, followed by an L-X-Y-C lipoprotein signal peptidase cleavage site. LipL36 is solubilized by Triton X-114 extraction of L. kirschneri; phase separation results in partitioning of LipL36 exclusively into the hydrophobic, detergent phase. LipL36 is intrinsically labeled during incubation of L. kirschneri in media containing [ super(3)H]palmitate. Processing of LipL36 is inhibited by globomycin, a selective inhibitor of lipoprotein signal peptidase. After processing, LipL36 is exported to the outer membrane along with LipL41 and lipopolysaccharide. Unlike LipL41, there appears to be differential expression of LipL36. In early-log-phase cultures, LipL36 is one of the most abundant L. kirschneri proteins. However, LipL36 levels drop considerably beginning in mid-log phase. LipL36 expression in vivo was evaluated by examining the humoral immune response to leptospiral antigens in the hamster model of leptospirosis. Hamsters surviving challenge with culture-adapted virulent L. kirschneri generate a strong antibody response to LipL36. In contrast, sera from hamsters surviving challenge with host-adapted L. kirschneri do not recognize LipL36. These findings suggest that LipL36 expression is downregulated during mammalian infection, providing a marker for studying the mechanisms by which pathogenic Leptospira species adapt to the host environment.
We report the cloning of the gene encoding a 36-kDa leptospiral outer membrane lipoprotein, designated LipL36. We obtained the N-terminal amino acid sequence of a staphylococcal V8 proteolytic-digest fragment in order to design an oligonucleotide probe. A Lambda-Zap II library containing Eco RI fragments of Leptospira kirschneri DNA was screened, and a 2.3-kb DNA fragment which contained the entire structural lipL36 gene was identified. Several lines of evidence indicate that LipL36 is lipid modified in a manner similar to that of LipL41, a leptospiral outer membrane lipoprotein we described in a previous study (E. S. Shang, T. A. Summers, and D. A. Haake, Infect. Immun. 64:2322–2330, 1996). The deduced amino acid sequence of LipL36 would constitute a 364-amino-acid polypeptide with a 20-amino-acid signal peptide, followed by an L-X-Y-C lipoprotein signal peptidase cleavage site. LipL36 is solubilized by Triton X-114 extraction of L. kirschneri ; phase separation results in partitioning of LipL36 exclusively into the hydrophobic, detergent phase. LipL36 is intrinsically labeled during incubation of L. kirschneri in media containing [ 3 H]palmitate. Processing of LipL36 is inhibited by globomycin, a selective inhibitor of lipoprotein signal peptidase. After processing, LipL36 is exported to the outer membrane along with LipL41 and lipopolysaccharide. Unlike LipL41, there appears to be differential expression of LipL36. In early-log-phase cultures, LipL36 is one of the most abundant L. kirschneri proteins. However, LipL36 levels drop considerably beginning in mid-log phase. LipL36 expression in vivo was evaluated by examining the humoral immune response to leptospiral antigens in the hamster model of leptospirosis. Hamsters surviving challenge with culture-adapted virulent L. kirschneri generate a strong antibody response to LipL36. In contrast, sera from hamsters surviving challenge with host-adapted L. kirschneri do not recognize LipL36. These findings suggest that LipL36 expression is downregulated during mammalian infection, providing a marker for studying the mechanisms by which pathogenic Leptospira species adapt to the host environment.
Author Jay D. Pruetz
Theresa A. Summers
Mary K. Mazel
Ellen S. Shang
Carole A. Bolin
Adam M. McCoy
David A. Haake
Carleen Martinich
AuthorAffiliation Division of Infectious Diseases, West Los Angeles Veterans Affairs Medical Center, Los Angeles, California 90073 1 ; Department of Microbiology, Immunology, and Molecular Genetics, University of California—Los Angeles School of Medicine, Los Angeles, California 90095 2 ; and National Animal Disease Center, Agricultural Research Service, U.S. Department of Agriculture, Ames, Iowa 50010 3
AuthorAffiliation_xml – name: Division of Infectious Diseases, West Los Angeles Veterans Affairs Medical Center, Los Angeles, California 90073 1 ; Department of Microbiology, Immunology, and Molecular Genetics, University of California—Los Angeles School of Medicine, Los Angeles, California 90095 2 ; and National Animal Disease Center, Agricultural Research Service, U.S. Department of Agriculture, Ames, Iowa 50010 3
Author_xml – sequence: 1
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  surname: HAAKE
  fullname: HAAKE, D. A
  organization: Division of Infectious Diseases, West Los Angeles Veterans Affairs Medical Center, Los Angeles, California 90073, United States
– sequence: 2
  givenname: C
  surname: MARTINICH
  fullname: MARTINICH, C
  organization: Division of Infectious Diseases, West Los Angeles Veterans Affairs Medical Center, Los Angeles, California 90073, United States
– sequence: 3
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  surname: SUMMERS
  fullname: SUMMERS, T. A
  organization: Division of Infectious Diseases, West Los Angeles Veterans Affairs Medical Center, Los Angeles, California 90073, United States
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  givenname: E. S
  surname: SHANG
  fullname: SHANG, E. S
  organization: Department of Microbiology, Immunology, and Molecular Genetics, University of California-Los Angeles School of Medicine, Los Angeles, California 90095, United States
– sequence: 5
  givenname: J. D
  surname: PRUETZ
  fullname: PRUETZ, J. D
  organization: Division of Infectious Diseases, West Los Angeles Veterans Affairs Medical Center, Los Angeles, California 90073, United States
– sequence: 6
  givenname: A. M
  surname: MCCOY
  fullname: MCCOY, A. M
  organization: Division of Infectious Diseases, West Los Angeles Veterans Affairs Medical Center, Los Angeles, California 90073, United States
– sequence: 7
  givenname: M. K
  surname: MAZEL
  fullname: MAZEL, M. K
  organization: Division of Infectious Diseases, West Los Angeles Veterans Affairs Medical Center, Los Angeles, California 90073, United States
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  surname: BOLIN
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  organization: National Animal Disease Center, Agricultural Research Service, U.S. Department of Agriculture, Ames, Iowa 50010, United States
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https://www.ncbi.nlm.nih.gov/pubmed/9529084$$D View this record in MEDLINE/PubMed
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Issue 4
Keywords Membrane protein
Spirochaetales
Host agent relation
Lipoprotein
Gene expression
External membrane
Characterization
Gene
Leptospiraceae
Bacteria
Molecular cloning
Structural analysis
Leptospira
Language English
License CC BY 4.0
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Editor: J. R. McGhee
Corresponding author. Mailing address: Division of Infectious Diseases, 111F, West Los Angeles Veterans Affairs Medical Center, Los Angeles, CA 90073. Phone: (310) 478-3711, ext. 40267. Fax: (310) 268-4928. E-mail: dhaake@ucla.edu.
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PublicationTitle Infection and Immunity
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PublicationYear 1998
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Snippet Classifications Services IAI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit...
We report the cloning of the gene encoding a 36-kDa leptospiral outer membrane lipoprotein, designated LipL36. We obtained the N-terminal amino acid sequence...
ABSTRACT We report the cloning of the gene encoding a 36-kDa leptospiral outer membrane lipoprotein, designated LipL36. We obtained the N-terminal amino acid...
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StartPage 1579
SubjectTerms Amino Acid Sequence
Animals
Anti-Bacterial Agents - pharmacology
Antibodies, Bacterial - blood
Bacterial Outer Membrane Proteins - genetics
Bacteriology
Base Sequence
Biological and medical sciences
Cricetinae
Down-Regulation
Female
Fundamental and applied biological sciences. Psychology
Leptospira - chemistry
Leptospira - growth & development
Leptospira - immunology
Leptospirosis - metabolism
Male
Mesocricetus
Mice
Microbiology
Molecular and Cellular Pathogenesis
Molecular Sequence Data
Octoxynol - pharmacology
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
Peptides
Solubility
Title Characterization of Leptospiral Outer Membrane Lipoprotein LipL36: Downregulation Associated with Late-Log-Phase Growth and Mammalian Infection
URI http://iai.asm.org/content/66/4/1579.abstract
https://www.ncbi.nlm.nih.gov/pubmed/9529084
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https://pubmed.ncbi.nlm.nih.gov/PMC108091
Volume 66
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