N-Terminal ArgD Peptides from the Classical Staphylococcus aureus Agr System Have Cytotoxic and Proinflammatory Activities

被引：20

作者：

Gonzalez, David J. ^{[1
,2
]}

Corriden, Ross ^{[3
]}

Akong-Moore, Kathryn ^{[3
]}

Olson, Joshua ^{[3
]}

Dorrestein, Pieter C. ^{[1
,2
,4
]}

Nizet, Victor ^{[2
,3
]}

机构：

[1] Univ Calif San Diego, Dept Pharmacol, La Jolla, CA 92093 USA

[2] Univ Calif San Diego, Skaggs Sch Pharm & Pharmaceut Sci, La Jolla, CA 92093 USA

[3] Univ Calif San Diego, Dept Pediat, La Jolla, CA 92093 USA

[4] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA

来源：

CHEMISTRY & BIOLOGY | 2014年 / 21卷 / 11期

关键词：

MASS-SPECTROMETRY; MOLECULAR NETWORKING; VIRULENCE; IDENTIFICATION; MRSA; EXPRESSION; SEQUENCE;

D O I：

10.1016/j.chembiol.2014.09.015

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

AgrD is the precursor for the autoinducing peptide in a quorum-sensing system regulating virulence phenotypes of the preeminent pathogen Staphylococcus aureus. Mass spectrometry-based methods, including molecular networking, identified formylated and nonformylated peptide variants derived from the AgrD N-terminal leader domain in S. aureus cell-free culture supernatants. Functional assessment of these peptides revealed unexpected bioactivities, including human cell-line cytotoxicity, modulation of neutrophil chemotaxis, neutrophil extracellular trap formation, and the aggravation of skin lesions in vivo.

引用

页码：1457 / 1462

页数：6

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