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PMID: 10075974 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

An inflammatory polypeptide complex from Staphylococcus epidermidis: isolation and characterization.

The Journal of experimental medicine ·Vol. 189 ·No. 6 ·1999-03-15 ·Pages 907-18

Mehlin C, Headley CM, Klebanoff SJ

Abstract

Staphylococcus epidermidis releases factors that activate the HIV-1 long terminal repeat, induce cytokine release, and activate nuclear factor B in cells of macrophage lineage. The active material had a mass of 34,500 daltons, was inactivated by proteases and partitioned into the phenol layer on hot aqueous phenol extraction, and thus was termed phenol-soluble modulin (PSM). High performance liquid chromatography (HPLC) of crude PSM yielded two peaks of activity designated PSM peak 1 and peak 2. MALDI-TOF (matrix-assisted laser desorption ionization-time of flight) mass spectroscopy indicated the presence of two components in peak 1, which were designated PSM and PSM. Peak 2 contained a single component, designated PSM. Separation of PSM and PSM in peak 1 could be achieved by a second HPLC procedure. The structure of each component was determined by amino acid sequence analysis and identification and sequencing of their genes. PSM, PSM, and PSM were 22-, 44-, and 25-amino acid, respectively, strongly hydrophobic polypeptides. PSM was identified as Staphylococcus epidermidis delta toxin, whereas PSM and PSM exhibited more distant homology to previously described staphylococcal toxins. They appeared to exist as a complex or aggregate with activity greater than the component parts. The properties of the S. epidermidis PSMs suggest that they may contribute to the systemic manifestations of Gram-positive sepsis.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/chemistry,genetics,isolation & purification Base Sequence Cell Line Cytokines/biosynthesis HIV Long Terminal Repeat Humans Lipopolysaccharides/pharmacology Molecular Sequence Data Molecular Weight NF-kappa B/metabolism Staphylococcus epidermidis/chemistry Teichoic Acids/pharmacology
Chemicals
Bacterial Proteins Cytokines Lipopolysaccharides NF-kappa B Teichoic Acids lipoteichoic acid
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Mehlin C
Department of Pathobiology, University of Washington, Seattle, Washington 98195, USA.
Headley C M
Klebanoff S J
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Article Info
Journal
The Journal of experimental medicine
Abbr.
J Exp Med
ISSN
0022-1007
DOI
10.1084/jem.189.6.907
Published
1999-03-15
Pages
907-18
Language
English
Region
United States
NLM ID
2985109R
PMCID
PMC2193041
Subset
IM
Grants
NIAID NIH HHS · AI07763 · United States
External Links
PubMed source DOI: 10.1084/jem.189.6.907 PMC Full Text View journal details
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