Identification of critical amino acid residues in the plague biofilm Hms proteins.

Identification of critical amino acid residues in the plague biofilm Hms proteins. Research Abstract Details 

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Identification of critical amino acid residues in the plague biofilm Hms proteins. Abstract Text:

Stanislav Forman,Alexander G Bobrov,Olga Kirillina,Susannah K Craig,Jennifer Abney,Jacqueline D Fetherston,Robert D Perry,

Yersinia pestis biofilm formation causes massive adsorption of haemin or Congo red in vitro as well as colonization and eventual blockage of the flea proventriculus in vivo. This blockage allows effective transmission of plague from some fleas, like the oriental rat flea, to mammals. Four Hms proteins, HmsH, HmsF, HmsR and HmsS, are essential for biofilm formation, with HmsT and HmsP acting as positive and negative regulators, respectively. HmsH has a beta-barrel structure with a large periplasmic domain while HmsF possesses polysaccharide deacetylase and COG1649 domains. HmsR is a putative glycosyltransferase while HmsS has no recognized domains. In this study, specific amino acids within conserved domains or within regions of high similarity in HmsH, HmsF, HmsR and HmsS proteins were selected for site-directed mutagenesis. Some but not all of the substitutions in HmsS and within the periplasmic domain of HmsH were critical for protein function. Substitutions within the glycosyltransferase domain of HmsR and the deacetylase domain of HmsF abolished biofilm formation in Y. pestis. Surprisingly, substitution of highly conserved residues within COG1649 did not affect HmsF function.

Identification of critical amino acid residues in the plague biofilm Hms proteins. Publishing Authors By Initials

S Forman,AG Bobrov,O Kirillina,SK Craig,J Abney,JD Fetherston,RD Perry,

For similar bacteria: gram-negative bacteria: gram-negative facultatively anaerobic rods: enterobacteriaceae: yersinia: yersinia pestis research abstracts see: bacteria: gram-negative bacteria: gram-negative facultatively anaerobic rods: enterobacteriaceae: yersinia: yersinia pestis research

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Identification of critical amino acid residues in the plague biofilm Hms proteins. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Microbiology (Reading, England)

VOLUME: 152

Page Numbers: 3399-410

Journal Abbreviation: Microbiology (Reading, Engl.)

ISSN: 1350-0872

DAY: 3

MONTH: Nov

YEAR: 2006

Identification of critical amino acid residues in the plague biofilm Hms proteins. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9430468

Identification of critical amino acid residues in the plague biofilm Hms proteins. Keywords Mesh Terms:

KEYWORDS: Yersinia pestis

MESH TERMS: physiology

Chemical & Substance for Abstract: Identification of critical amino acid residues in the plague biofilm Hms proteins. Information

Substance Name: Glycosyltransferases

Registry Number: EC 2.4.-

Grant and Affiliation Information for Identification of critical amino acid residues in the plague biofilm Hms proteins.

AFFILIATION: Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky, Lexington, KY 40536-0084, USA.

Country: England

AGENCY: United States NIAID

GRANT: AI25098

ACRONYM: AI

MEDLINETA: Microbiology

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