Edwardsiella tarda MliC, a lysozyme inhibitor that participates in pathogenesis in a manner that parallels Ivy
Edwardsiella tarda, a bacterial pathogen to farmed fish as well as humans, possesses the genes of two lysozyme inhibitors, ivy and mliC (ivy(Et) and mliC(Et)). We recently studied IvyEt and found it to be implicated in E. tarda virulence. In the present study, we characterized MliC(Et) in comparison...
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Published in | Infection and immunity Vol. 83; no. 2; pp. 583 - 590 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
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American Society for Microbiology
01.02.2015
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Abstract | Edwardsiella tarda, a bacterial pathogen to farmed fish as well as humans, possesses the genes of two lysozyme inhibitors, ivy and mliC (ivy(Et) and mliC(Et)). We recently studied IvyEt and found it to be implicated in E. tarda virulence. In the present study, we characterized MliC(Et) in comparison with Ivy(Et) in a turbot model. MliC(Et) contains the FWSKG motif and two cysteines (C33 and C98) that are highly conserved in subgroup 1 MliCs but are of unknown functional importance. To examine the essentialness of these conserved structural features, recombinant MliC(Et) (rMliC) and its mutants bearing C33S and W79A (of the FWSKG motif) substitutions were prepared. Subsequent analysis showed that rMliC (i) inhibited lysozyme-induced lysis of a Gram-positive bacterium, (ii) reduced serum-facilitated lysozyme killing of E. tarda, and (iii) when introduced into turbot, promoted bacterial dissemination in fish tissues. The C33S mutation had no influence on the activity of rMliC, while the W79A mutation slightly but significantly enhanced the activity of rMliC. Knockout strains of either mliC(Et) or ivy(Et) were severely attenuated for the ability of tissue invasion, host lethality, serum survival, and intracellular replication. The lost virulence of the mliC transformant (TXΔmliC) was restored by complementation with an introduced mliC(Et) gene. Compared to the Δivy(Et) or ΔmliC(Et) single-knockout strains, the ΔmliC(Et) Δivy(Et) double-knockout strain was significantly impaired in most of the virulence features. Together, these results provide the first evidence that the conserved cysteine is functionally dispensable to a subgroup 1 MliC and that as a virulence factor, MliC(Et) most likely works in a concerted and parallel manner with Ivy. |
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AbstractList | ABSTRACT
Edwardsiella tarda
, a bacterial pathogen to farmed fish as well as humans, possesses the genes of two lysozyme inhibitors,
ivy
and
mliC
(
ivy
Et
and
mliC
Et
). We recently studied Ivy
Et
and found it to be implicated in
E. tarda
virulence. In the present study, we characterized MliC
Et
in comparison with Ivy
Et
in a turbot model. MliC
Et
contains the FWSKG motif and two cysteines (C33 and C98) that are highly conserved in subgroup 1 MliCs but are of unknown functional importance. To examine the essentialness of these conserved structural features, recombinant MliC
Et
(rMliC) and its mutants bearing C33S and W79A (of the FWSKG motif) substitutions were prepared. Subsequent analysis showed that rMliC (i) inhibited lysozyme-induced lysis of a Gram-positive bacterium, (ii) reduced serum-facilitated lysozyme killing of
E. tarda
, and (iii) when introduced into turbot, promoted bacterial dissemination in fish tissues. The C33S mutation had no influence on the activity of rMliC, while the W79A mutation slightly but significantly enhanced the activity of rMliC. Knockout strains of either
mliC
Et
or
ivy
Et
were severely attenuated for the ability of tissue invasion, host lethality, serum survival, and intracellular replication. The lost virulence of the
mliC
transformant (TXΔ
mliC
) was restored by complementation with an introduced
mliC
Et
gene. Compared to the Δ
ivy
Et
or Δ
mliC
Et
single-knockout strains, the Δ
mliC
Et
Δ
ivy
Et
double-knockout strain was significantly impaired in most of the virulence features. Together, these results provide the first evidence that the conserved cysteine is functionally dispensable to a subgroup 1 MliC and that as a virulence factor, MliC
Et
most likely works in a concerted and parallel manner with Ivy. Edwardsiella tarda , a bacterial pathogen to farmed fish as well as humans, possesses the genes of two lysozyme inhibitors, ivy and mliC ( ivy Et and mliC Et ). We recently studied Ivy Et and found it to be implicated in E. tarda virulence. In the present study, we characterized MliC Et in comparison with Ivy Et in a turbot model. MliC Et contains the FWSKG motif and two cysteines (C33 and C98) that are highly conserved in subgroup 1 MliCs but are of unknown functional importance. To examine the essentialness of these conserved structural features, recombinant MliC Et (rMliC) and its mutants bearing C33S and W79A (of the FWSKG motif) substitutions were prepared. Subsequent analysis showed that rMliC (i) inhibited lysozyme-induced lysis of a Gram-positive bacterium, (ii) reduced serum-facilitated lysozyme killing of E. tarda , and (iii) when introduced into turbot, promoted bacterial dissemination in fish tissues. The C33S mutation had no influence on the activity of rMliC, while the W79A mutation slightly but significantly enhanced the activity of rMliC. Knockout strains of either mliC Et or ivy Et were severely attenuated for the ability of tissue invasion, host lethality, serum survival, and intracellular replication. The lost virulence of the mliC transformant (TXΔ mliC ) was restored by complementation with an introduced mliC Et gene. Compared to the Δ ivy Et or Δ mliC Et single-knockout strains, the Δ mliC Et Δ ivy Et double-knockout strain was significantly impaired in most of the virulence features. Together, these results provide the first evidence that the conserved cysteine is functionally dispensable to a subgroup 1 MliC and that as a virulence factor, MliC Et most likely works in a concerted and parallel manner with Ivy. Edwardsiella tarda, a bacterial pathogen to farmed fish as well as humans, possesses the genes of two lysozyme inhibitors, ivy and mliC (ivy(Et) and mliC(Et)). We recently studied IvyEt and found it to be implicated in E. tarda virulence. In the present study, we characterized MliC(Et) in comparison with Ivy(Et) in a turbot model. MliC(Et) contains the FWSKG motif and two cysteines (C33 and C98) that are highly conserved in subgroup 1 MliCs but are of unknown functional importance. To examine the essentialness of these conserved structural features, recombinant MliC(Et) (rMliC) and its mutants bearing C33S and W79A (of the FWSKG motif) substitutions were prepared. Subsequent analysis showed that rMliC (i) inhibited lysozyme-induced lysis of a Gram-positive bacterium, (ii) reduced serum-facilitated lysozyme killing of E. tarda, and (iii) when introduced into turbot, promoted bacterial dissemination in fish tissues. The C33S mutation had no influence on the activity of rMliC, while the W79A mutation slightly but significantly enhanced the activity of rMliC. Knockout strains of either mliC(Et) or ivy(Et) were severely attenuated for the ability of tissue invasion, host lethality, serum survival, and intracellular replication. The lost virulence of the mliC transformant (TXΔmliC) was restored by complementation with an introduced mliC(Et) gene. Compared to the Δivy(Et) or ΔmliC(Et) single-knockout strains, the ΔmliC(Et) Δivy(Et) double-knockout strain was significantly impaired in most of the virulence features. Together, these results provide the first evidence that the conserved cysteine is functionally dispensable to a subgroup 1 MliC and that as a virulence factor, MliC(Et) most likely works in a concerted and parallel manner with Ivy. Edwardsiella tarda, a bacterial pathogen to farmed fish as well as humans, possesses the genes of two lysozyme inhibitors, ivy and mliC (ivyEt and mliCEt). We recently studied IvyEt and found it to be implicated in E. tarda virulence. In the present study, we characterized MliCEt in comparison with IvyEt in a turbot model. MliCEt contains the FWSKG motif and two cysteines (C33 and C98) that are highly conserved in subgroup 1 MliCs but are of unknown functional importance. To examine the essentialness of these conserved structural features, recombinant MliCEt (rMliC) and its mutants bearing C33S and W79A (of the FWSKG motif) substitutions were prepared. Subsequent analysis showed that rMliC (i) inhibited lysozyme-induced lysis of a Gram-positive bacterium, (ii) reduced serum-facilitated lysozyme killing of E. tarda, and (iii) when introduced into turbot, promoted bacterial dissemination in fish tissues. The C33S mutation had no influence on the activity of rMliC, while the W79A mutation slightly but significantly enhanced the activity of rMliC. Knockout strains of either mliCEt or ivyEt were severely attenuated for the ability of tissue invasion, host lethality, serum survival, and intracellular replication. The lost virulence of the mliC transformant (TX Delta mliC) was restored by complementation with an introduced mliCEt gene. Compared to the Delta ivyEt or Delta mliCEt single-knockout strains, the Delta mliCEt Delta ivyEt double-knockout strain was significantly impaired in most of the virulence features. Together, these results provide the first evidence that the conserved cysteine is functionally dispensable to a subgroup 1 MliC and that as a virulence factor, MliCEt most likely works in a concerted and parallel manner with Ivy. |
Author | Li, Mo-Fei Sun, Li Wang, Chong |
Author_xml | – sequence: 1 givenname: Mo-Fei surname: Li fullname: Li, Mo-Fei organization: Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, China University of Chinese Academy of Sciences, Beijing, China – sequence: 2 givenname: Chong surname: Wang fullname: Wang, Chong organization: Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, China University of Chinese Academy of Sciences, Beijing, China – sequence: 3 givenname: Li surname: Sun fullname: Sun, Li email: lsun@qdio.ac.cn organization: Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, China Collaborative Innovation Center of Deep Sea Biology, Zhejiang University, Hangzhou, China lsun@qdio.ac.cn |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Citation Li M-F, Wang C, Sun L. 2015. Edwardsiella tarda MliC, a lysozyme inhibitor that participates in pathogenesis in a manner that parallels Ivy. Infect Immun 83:583–590. doi:10.1128/IAI.02473-14. |
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Snippet | Edwardsiella tarda, a bacterial pathogen to farmed fish as well as humans, possesses the genes of two lysozyme inhibitors, ivy and mliC (ivy(Et) and mliC(Et)).... ABSTRACT Edwardsiella tarda , a bacterial pathogen to farmed fish as well as humans, possesses the genes of two lysozyme inhibitors, ivy and mliC ( ivy Et and... Edwardsiella tarda, a bacterial pathogen to farmed fish as well as humans, possesses the genes of two lysozyme inhibitors, ivy and mliC (ivyEt and mliCEt). We... Edwardsiella tarda , a bacterial pathogen to farmed fish as well as humans, possesses the genes of two lysozyme inhibitors, ivy and mliC ( ivy Et and mliC Et... |
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SubjectTerms | Animals Bacterial Infections Bacterial Proteins - genetics Base Sequence Edwardsiella tarda Edwardsiella tarda - pathogenicity Enterobacteriaceae Infections - immunology Enterobacteriaceae Infections - pathology Enterobacteriaceae Infections - veterinary Fish Diseases - microbiology Flatfishes - microbiology Gene Expression Regulation, Bacterial Gene Knockout Techniques Kidney - cytology Monocytes - microbiology Muramidase - antagonists & inhibitors Recombinant Proteins - genetics Recombinant Proteins - pharmacology Scophthalmus maximus Sequence Analysis, DNA Virulence Factors - genetics |
Title | Edwardsiella tarda MliC, a lysozyme inhibitor that participates in pathogenesis in a manner that parallels Ivy |
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