Silkworm apolipophorin protein inhibits hemolysin gene expression of staphylococcus aureus via binding to cell surface lipoteichoic acids

Yosuke Omae; Yuichi Hanada; Kazuhisa Sekimizu; Chikara Kaito

doi:10.1074/jbc.M113.495051

Silkworm apolipophorin protein inhibits hemolysin gene expression of staphylococcus aureus via binding to cell surface lipoteichoic acids

Yosuke Omae, Yuichi Hanada, Kazuhisa Sekimizu, Chikara Kaito

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

Abstract

Background: Silkworm ApoLp protein binds S. aureus cell surfaces and inhibits hemolysin gene expression. Results: ApoLp protein binds LTA. The ApoLp inhibitory effect was attenuated in an LTA synthetase knockdown mutant. Conclusion: ApoLp protein suppressed S. aureus virulence via LTA binding. Significance: A non-protein macromolecule on the bacterial cell surface functions as a receptor in the bacterial signal transduction pathway.

Original language	English
Pages (from-to)	25542-25550
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	288
Issue number	35
DOIs	https://doi.org/10.1074/jbc.M113.495051
Publication status	Published - Aug 30 2013
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1074/jbc.M113.495051

Cite this

@article{c22cbd7b6c0f4c3dadbb773ac63b3388,

title = "Silkworm apolipophorin protein inhibits hemolysin gene expression of staphylococcus aureus via binding to cell surface lipoteichoic acids",

abstract = "Background: Silkworm ApoLp protein binds S. aureus cell surfaces and inhibits hemolysin gene expression. Results: ApoLp protein binds LTA. The ApoLp inhibitory effect was attenuated in an LTA synthetase knockdown mutant. Conclusion: ApoLp protein suppressed S. aureus virulence via LTA binding. Significance: A non-protein macromolecule on the bacterial cell surface functions as a receptor in the bacterial signal transduction pathway.",

author = "Yosuke Omae and Yuichi Hanada and Kazuhisa Sekimizu and Chikara Kaito",

year = "2013",

month = aug,

day = "30",

doi = "10.1074/jbc.M113.495051",

language = "English",

volume = "288",

pages = "25542--25550",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "35",

}

TY - JOUR

T1 - Silkworm apolipophorin protein inhibits hemolysin gene expression of staphylococcus aureus via binding to cell surface lipoteichoic acids

AU - Omae, Yosuke

AU - Hanada, Yuichi

AU - Sekimizu, Kazuhisa

AU - Kaito, Chikara

PY - 2013/8/30

Y1 - 2013/8/30

N2 - Background: Silkworm ApoLp protein binds S. aureus cell surfaces and inhibits hemolysin gene expression. Results: ApoLp protein binds LTA. The ApoLp inhibitory effect was attenuated in an LTA synthetase knockdown mutant. Conclusion: ApoLp protein suppressed S. aureus virulence via LTA binding. Significance: A non-protein macromolecule on the bacterial cell surface functions as a receptor in the bacterial signal transduction pathway.

AB - Background: Silkworm ApoLp protein binds S. aureus cell surfaces and inhibits hemolysin gene expression. Results: ApoLp protein binds LTA. The ApoLp inhibitory effect was attenuated in an LTA synthetase knockdown mutant. Conclusion: ApoLp protein suppressed S. aureus virulence via LTA binding. Significance: A non-protein macromolecule on the bacterial cell surface functions as a receptor in the bacterial signal transduction pathway.

UR - http://www.scopus.com/inward/record.url?scp=84883349698&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84883349698&partnerID=8YFLogxK

U2 - 10.1074/jbc.M113.495051

DO - 10.1074/jbc.M113.495051

M3 - Article

C2 - 23873929

AN - SCOPUS:84883349698

SN - 0021-9258

VL - 288

SP - 25542

EP - 25550

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 35

ER -

Silkworm apolipophorin protein inhibits hemolysin gene expression of staphylococcus aureus via binding to cell surface lipoteichoic acids

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this