Home LiteratureArticle Details
PMID: 7914665 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Longus: a long pilus ultrastructure produced by human enterotoxigenic Escherichia coli.

Molecular microbiology ·Vol. 12 ·No. 1 ·1994-04-00 ·Pages 71-82

Girón JA, Levine MM, Kaper JB

Abstract

Enterotoxigenic Escherichia coli (ETEC) causes an acute cholera-like diarrhoea in both humans and animals. We describe a new pilus termed longus produced by ETEC, which can extend for over 20 microns from the cell surface. Longus is composed of a repeating subunit of 22 kDa and its NH2-terminal amino acid sequence revealed homology with the toxin-coregulated pilus of Vibrio cholerae, the bundle-forming pilus of enteropathogenic E. coli and type IV pilins of some Gram-negative bacterial pathogens. The longus structural gene (lngA) is encoded in a large plasmid and was cloned in a 5 kb fragment, which proved to be sufficient for pilus production and assembly in E. coli K-12. The presence of lngA was restricted to human ETEC strains. In contrast to other ETEC pili, lngA was widely distributed among ETEC strains independent of their geographical origin, serotype, toxin production, or other pili antigens expressed. Longus is a new member of the type IV pili family, which may represent a highly conserved intestinal colonization factor of ETEC. Common antigenic determinants exist among longus and their pilin subunits, produced by heterologous ETEC. Longus could be significant in the immunoprophylaxis of diarrhoeal disease caused by ETEC, especially against those strains in which no colonization factors have been identified and that produce heat-stable toxin only.

Related Genes
MeSH Terms
Amino Acid Sequence Bacterial Adhesion Bacterial Toxins/metabolism Base Sequence Cell Line Enterotoxins/metabolism Escherichia coli/pathogenicity,ultrastructure Escherichia coli Proteins Fimbriae, Bacterial/ultrastructure Hemagglutination Humans Molecular Sequence Data Sequence Alignment Sequence Homology, Amino Acid Virulence
Chemicals
Bacterial Toxins Enterotoxins Escherichia coli Proteins heat stable toxin (E coli) heat-labile enterotoxin, E coli
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Girón J A
Center for Vaccine Development, School of Medicine, University of Maryland, Baltimore 21201.
Levine M M
Kaper J B
Article Info
Journal
Molecular microbiology
Abbr.
Mol Microbiol
ISSN
0950-382X
Published
1994-04-00
Pages
71-82
Language
English
Region
England
NLM ID
8712028
Subset
IM
Grants
NIAID NIH HHS · R37 AI021657 · United States
NIAID NIH HHS · AI21657 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com