Molecular characterization of the oafA locus responsible for acetylation of Salmonella typhimurium O-antigen: OafA is a member of a family of integral membrane trans-acylases

James M. Slauch, Angela A. Lee, Michael J. Mahan, John J. Mekalanos

Research output: Contribution to journalArticle

Abstract

Lipopolysaccharide (LPS) coats the surface of gram-negative bacteria and serves to protect the cell from its environment. The O-antigen is the outermost part of LPS and is highly variable among gram-negative bacteria. Strains of Salmonella are partly distinguished by serotypic differences in their O-antigen. In Salmonella typhimurium, the O-antigen is acetylated, conferring the O5 serotype. We have previously provided evidence that this modification significantly alters the structure of the O-antigen and creates or destroys a series of conformational epitopes. Here we report the detailed mapping, cloning, and DNA sequence of the oafA gene. The locus contains one open reading frame that is predicted to encode an inner membrane protein, consistent with its role in modification of the O-antigen subunit. The OafA protein shows homology to proteins in a number of prokaryotic and one eukaryotic species, and this defines a family of membrane proteins involved in the acylation of exported carbohydrate moieties. In many of these instances, acylation defines serotype or host range and thus has a profound effect on microbe-host interaction.

Original languageEnglish (US)
Pages (from-to)5904-5909
Number of pages6
JournalJournal of bacteriology
Volume178
Issue number20
DOIs
StatePublished - Jan 1 1996

Fingerprint

amidase
O Antigens
Salmonella typhimurium
Acetylation
Membranes
Acylation
Gram-Negative Bacteria
Lipopolysaccharides
Membrane Proteins
Host Specificity
Salmonella
Open Reading Frames
Organism Cloning
Epitopes
Proteins
Carbohydrates

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

Molecular characterization of the oafA locus responsible for acetylation of Salmonella typhimurium O-antigen : OafA is a member of a family of integral membrane trans-acylases. / Slauch, James M.; Lee, Angela A.; Mahan, Michael J.; Mekalanos, John J.

In: Journal of bacteriology, Vol. 178, No. 20, 01.01.1996, p. 5904-5909.

Research output: Contribution to journalArticle

@article{dbe7424a9ad74ecb90aaba5f8ec3e8a7,
title = "Molecular characterization of the oafA locus responsible for acetylation of Salmonella typhimurium O-antigen: OafA is a member of a family of integral membrane trans-acylases",
abstract = "Lipopolysaccharide (LPS) coats the surface of gram-negative bacteria and serves to protect the cell from its environment. The O-antigen is the outermost part of LPS and is highly variable among gram-negative bacteria. Strains of Salmonella are partly distinguished by serotypic differences in their O-antigen. In Salmonella typhimurium, the O-antigen is acetylated, conferring the O5 serotype. We have previously provided evidence that this modification significantly alters the structure of the O-antigen and creates or destroys a series of conformational epitopes. Here we report the detailed mapping, cloning, and DNA sequence of the oafA gene. The locus contains one open reading frame that is predicted to encode an inner membrane protein, consistent with its role in modification of the O-antigen subunit. The OafA protein shows homology to proteins in a number of prokaryotic and one eukaryotic species, and this defines a family of membrane proteins involved in the acylation of exported carbohydrate moieties. In many of these instances, acylation defines serotype or host range and thus has a profound effect on microbe-host interaction.",
author = "Slauch, {James M.} and Lee, {Angela A.} and Mahan, {Michael J.} and Mekalanos, {John J.}",
year = "1996",
month = "1",
day = "1",
doi = "10.1128/jb.178.20.5904-5909.1996",
language = "English (US)",
volume = "178",
pages = "5904--5909",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "20",

}

TY - JOUR

T1 - Molecular characterization of the oafA locus responsible for acetylation of Salmonella typhimurium O-antigen

T2 - OafA is a member of a family of integral membrane trans-acylases

AU - Slauch, James M.

AU - Lee, Angela A.

AU - Mahan, Michael J.

AU - Mekalanos, John J.

PY - 1996/1/1

Y1 - 1996/1/1

N2 - Lipopolysaccharide (LPS) coats the surface of gram-negative bacteria and serves to protect the cell from its environment. The O-antigen is the outermost part of LPS and is highly variable among gram-negative bacteria. Strains of Salmonella are partly distinguished by serotypic differences in their O-antigen. In Salmonella typhimurium, the O-antigen is acetylated, conferring the O5 serotype. We have previously provided evidence that this modification significantly alters the structure of the O-antigen and creates or destroys a series of conformational epitopes. Here we report the detailed mapping, cloning, and DNA sequence of the oafA gene. The locus contains one open reading frame that is predicted to encode an inner membrane protein, consistent with its role in modification of the O-antigen subunit. The OafA protein shows homology to proteins in a number of prokaryotic and one eukaryotic species, and this defines a family of membrane proteins involved in the acylation of exported carbohydrate moieties. In many of these instances, acylation defines serotype or host range and thus has a profound effect on microbe-host interaction.

AB - Lipopolysaccharide (LPS) coats the surface of gram-negative bacteria and serves to protect the cell from its environment. The O-antigen is the outermost part of LPS and is highly variable among gram-negative bacteria. Strains of Salmonella are partly distinguished by serotypic differences in their O-antigen. In Salmonella typhimurium, the O-antigen is acetylated, conferring the O5 serotype. We have previously provided evidence that this modification significantly alters the structure of the O-antigen and creates or destroys a series of conformational epitopes. Here we report the detailed mapping, cloning, and DNA sequence of the oafA gene. The locus contains one open reading frame that is predicted to encode an inner membrane protein, consistent with its role in modification of the O-antigen subunit. The OafA protein shows homology to proteins in a number of prokaryotic and one eukaryotic species, and this defines a family of membrane proteins involved in the acylation of exported carbohydrate moieties. In many of these instances, acylation defines serotype or host range and thus has a profound effect on microbe-host interaction.

UR - http://www.scopus.com/inward/record.url?scp=0029837945&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029837945&partnerID=8YFLogxK

U2 - 10.1128/jb.178.20.5904-5909.1996

DO - 10.1128/jb.178.20.5904-5909.1996

M3 - Article

C2 - 8830685

AN - SCOPUS:0029837945

VL - 178

SP - 5904

EP - 5909

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 20

ER -