A Streptococcus suis LysM domain surface protein contributes to bacterial virulence

Veterinary Microbiology

Volumn 187, Issue , 2016, Pages 64-69

  Wu, Zongfu ^a,b   Shao, Jing ^a,b,e   Ren, Haiyan ^a,b   Tang, Huanyu ^a,b   Zhou, Mingyao ^a,b   Dai, Jiao ^a,b   Lai, Liying ^a,b   Yao, Huochun ^a,b   Fan, Hongjie ^a,b,c   Chen, Dai ^d   Zong, Jie ^d   Lu, Chengping ^a,b  

^a NANJING AGRICULTURAL UNIVERSITY   (China)

^b AGRO ENVIRONMENTAL PROTECTION INSTITUTE   (China)

^c YANGZHOU UNIVERSITY   (China)

^d Novel Bioinformatics Company   (China)

^e Sichuan Animal Disease Control Center   (China)

Author keywords

Bacterial virulence; Iron; LysM domain; Streptococcus suis

Indexed keywords

BACTERIAL PROTEIN; BACTERIAL VACCINE; IRON BINDING PROTEIN; LYSM PROTEIN; MEMBRANE PROTEIN; STREPTOCOCCUS ANTIGEN; TRANSCRIPTOME; UNCLASSIFIED DRUG; IRON; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; BACTERIAL STRAIN; BACTERIAL VIRULENCE; CONTROLLED STUDY; DELETION MUTANT; GENE EXPRESSION; IRON KINETICS; MOUSE; NONHUMAN; PATHOGENESIS; STREPTOCOCCUS AGALACTIAE; STREPTOCOCCUS INFECTION; STREPTOCOCCUS SUIS; STREPTOCOCCUS SUIS INFECTION; BLOOD; CHEMISTRY; GENETICS; HOST PATHOGEN INTERACTION; IMMUNOLOGY; METABOLISM; MICROBIAL VIABILITY; MICROBIOLOGY; PATHOGENICITY; PHYSIOLOGY; SEQUENCE HOMOLOGY; VIRULENCE;

AMINO ACID SEQUENCE; BACTERIAL VACCINES; BLOOD; HOST-PATHOGEN INTERACTIONS; IRON; MEMBRANE PROTEINS; MICROBIAL VIABILITY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STREPTOCOCCUS SUIS; TRANSCRIPTOME; VIRULENCE;

EID: 84962214973     PISSN: 03781135     EISSN: 18732542     Source Type: Journal    
DOI: 10.1016/j.vetmic.2016.03.017     Document Type: Article

References (18)

1. Bateman A., Bycroft M. The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). J. Mol. Biol. 2000, 299:1113-1119.
2. Beineke A., Bennecke K., Neis C., Schroder C., Waldmann K.H., Baumgartner W., Valentin-Weigand P., Baums C.G. Comparative evaluation of virulence and pathology of Streptococcus suis serotypes 2 and 9 in experimentally infected growers. Vet. Microbiol. 2008, 128:423-430.
3. Brodeur B.R., Boyer M., Charlebois I., Hamel J., Couture F., Rioux C.R., Martin D. Identification of group B streptococcal Sip protein, which elicits cross-protective immunity. Infect. Immun. 2000, 68:5610-5618.
4. Chen H.Y., Shen H., Jia B., Zhang Y.S., Wang X.H., Zeng X.C. Differential gene expression in ovaries of Qira black sheep and Hetian sheep using RNA-Seq technique. PLoS One 2015, 10:e0120170.
5. Daou N., Buisson C., Gohar M., Vidic J., Bierne H., Kallassy M., Lereclus D., Nielsen-LeRoux C. IlsA, a unique surface protein of Bacillus cereus required for iron acquisition from heme, hemoglobin and ferritin. PLoS Pathog. 2009, 5:e1000675.
6. Eckert C., Lecerf M., Dubost L., Arthur M., Mesnage S. Functional analysis of AtlA, the major N-acetylglucosaminidase of Enterococcus faecalis. J. Bacteriol. 2006, 188:8513-8519.
7. Fittipaldi N., Segura M., Grenier D., Gottschalk M. Virulence factors involved in the pathogenesis of the infection caused by the swine pathogen and zoonotic agent Streptococcus suis. Future Microbiol. 2012, 7:259-279.
8. Jerse A.E., Yu J., Tall B.D., Kaper J.B. A genetic locus of enteropathogenic Escherichia coli necessary for the production of attaching and effacing lesions on tissue culture cells. Proc. Natl. Acad. Sci. U. S. A. 1990, 87:7839-7843.
9. Kerdsin A., Hatrongjit R., Gottschalk M., Takeuchi D., Hamada S., Akeda Y., Oishi K. Emergence of Streptococcus suis serotype 9 infection in humans. J. Microbiol. Immunol. Infect. 2015, 10.1016/j.jmii.2015.06.011.
10. Liu P., Pian Y., Li X., Liu R., Xie W., Zhang C., Zheng Y., Jiang Y., Yuan Y. Streptococcus suis adenosine synthase functions as an effector in evasion of PMN-mediated innate immunit. J. Infect. Dis. 2014, 210:35-45.
11. Ratledge C., Dover L.G. Iron metabolism in pathogenic bacteria. Annu. Rev. Microbiol. 2000, 54:881-941.
12. Ruhland G.J., Hellwig M., Wanner G., Fiedler F. Cell-surface location of Listeria-specific protein p60-detection of Listeria cells by indirect immunofluorescence. J. Gen. Microbiol. 1993, 139:609-616.
13. Turner M.S., Hafner L.M., Walsh T., Giffard P.M. Identification and characterization of the novel LysM domain-containing surface protein Sep from Lactobacillus fermentum BR11 and its use as a peptide fusion partner in Lactobacillus and Lactococcus. Appl. Environ. Microbiol. 2004, 70:3673-3680.
14. Uhlen M., Guss B., Nilsson B., Gatenbeck S., Philipson L., Lindberg M. Complete sequence of the staphylococcal gene encoding protein A: a gene evolved through multiple duplications. J. Biol. Chem. 1984, 259:1695-1702.
15. Wu Z., Zhang W., Lu C. Comparative proteome analysis of secreted proteins of Streptococcus suis serotype 9 isolates from diseased and healthy pigs. Microb. Pathog. 2008, 45:159-166.
16. Wu Z., Wang W., Tang M., Shao J., Dai C., Zhang W., Fan H., Yao H., Zong J., Chen D., Wang J., Lu C. Comparative genomic analysis shows that Streptococcus suis meningitis isolate SC070731 contains a unique 105K genomic island. Gene 2014, 535:156-164.
17. Wu Z., Wu C., Shao J., Zhu Z., Wang W., Zhang W., Tang M., Pei N., Fan H., Li J., Yao H., Gu H., Xu X., Lu C. The Streptococcus suis transcriptional landscape reveals adaptation mechanisms in pig blood and cerebrospinal fluid. RNA 2014, 20:882-898.
18. Zhu H., Huang D., Zhang W., Wu Z., Lu Y., Jia H., Wang M., Lu C. The novel virulence-related gene stp of Streptococcus suis serotype 9 strain contributes to a significant reduction in mouse mortality. Microb. Pathog. 2011, 51:442-453.