Donor strand complementation governs intersubunit interaction of fimbriae of the alternate chaperone pathway.

Donor strand complementation governs intersubunit interaction of fimbriae of the alternate chaperone pathway. Research Abstract Details 

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Donor strand complementation governs intersubunit interaction of fimbriae of the alternate chaperone pathway. Abstract Text:

Steven T Poole,Annette L McVeigh,Ravi P Anantha,Lanfong H Lee,Yasemin M Akay,Emily A Pontzer,Daniel A Scott,Esther Bullitt,Stephen J Savarino,

Fimbrial filaments assembled by distinct chaperone pathways share a common mechanism of intersubunit interaction, as elucidated for colonization factor antigen I (CFA/I), archetype of enterotoxigenic Escherichia coli (ETEC) Class 5 fimbriae. We postulated that a highly conserved beta-strand at the major subunit N-terminus represents the donor strand, analogous to interactions within Class I pili. We show here that CFA/I fimbriae utilize donor strand complementation to promote proper folding of and interactions between CFA/I subunits. We constructed a series of genetic variants of CfaE, the CFA/I adhesin, incorporating a C-terminal extension comprising a flexible linker and 10-19 of the N-terminal residues of CfaB, the major subunit. Variants with a donor strand complement (dsc) of >or= 12 residues were recoverable from periplasmic fractions. Genetic disruption of the donor beta-strand reduced CfaE recovery. A hexahistidine-tagged variant of dsc19CfaE formed soluble monomers, folded into beta-sheet conformation, displayed adhesion characteristic of CFA/I, and elicited antibodies that inhibited mannose-resistant haemagglutination by ETEC expressing CFA/I, CS4 and CS14 fimbriae. Immunoelectron microscopy indicated that CfaE was confined to the distal fimbrial tip. Our findings provide the basis to elucidate structure and function of this class of fimbrial adhesins and assess the feasibility of an adhesin-based vaccine.

Donor strand complementation governs intersubunit interaction of fimbriae of the alternate chaperone pathway. Publishing Authors By Initials

ST Poole,AL McVeigh,RP Anantha,LH Lee,YM Akay,EA Pontzer,DA Scott,E Bullitt,SJ Savarino,

For similar proteins: recombinant proteins research abstracts see: proteins: recombinant proteins research

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Donor strand complementation governs intersubunit interaction of fimbriae of the alternate chaperone pathway. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Molecular microbiology

VOLUME: 63

Page Numbers: 1372-84

Journal Abbreviation: Mol. Microbiol.

ISSN: 0950-382X

DAY: 3

MONTH: Mar

YEAR: 2007

Donor strand complementation governs intersubunit interaction of fimbriae of the alternate chaperone pathway. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8712028

Donor strand complementation governs intersubunit interaction of fimbriae of the alternate chaperone pathway. Keywords Mesh Terms:

KEYWORDS: Recombinant Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Donor strand complementation governs intersubunit interaction of fimbriae of the alternate chaperone pathway. Information

Substance Name: Fimbriae Proteins

Registry Number: 147680-16-8

Grant and Affiliation Information for Donor strand complementation governs intersubunit interaction of fimbriae of the alternate chaperone pathway.

AFFILIATION: Enteric Diseases Department, Naval Medical Research Center, 503 Robert Grant Avenue, Silver Spring, MD 20910, USA.

Country: England

AGENCY: United States NHLBI

GRANT: T32-HL07291

ACRONYM: HL

MEDLINETA: Mol Microbiol

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