Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/62805
Type: Artigo de periódico
Title: Characterization of a nonfimbrial mannose-sensitive hemagglutinin (MSH) produced by Salmonella enterica serovar Enteritidis
Author: Mikcha, JMG
Freire, MG
Macedo, MLR
Yano, T
Ferreira, AJP
Abstract: A nonfimbrial mannose-sensitive hemagglutinin (MSH) with adhesive properties produced by Salmonella enterica serovar Enteritidis was characterized. The MSH was characterized as glycoprotein and consisted of three noncovalently bound subunits of Mr 28, 33 and 40kDa determined by SDS-PAGE. The hemagglutinin was heat-stable and resistant to alkaline (high) or acid (low) pH, however, it was inhibited by proteolytic enzymes, by EDTA and by sodium periodate. Mouse antiserum raised against MSH reacted with the 28 kDa band in immunoblotting, and also inhibited hemagglutination and bacterial adherence to HeLa cells. Electron microscope examinations showed that MSH is not a fimbriae-like structure. MSH and anti-MSH IgG competitively inhibited bacterial adherence to HeLa cells. The immunofluorescence test, using MSH on HeLa cells and specific anti-MSH IgG, supported the view that MSH contributes to adherence of the organism. These results indicate that MSH is a nonfimbrial putative adhesive factor that may mediate the adherence of Salmonella enteritidis to eucaryotic cells. (c) 2006 Elsevier Ltd. All rights reserved.
Subject: Salmonella enteritidis
nonfimbrial hemagglutinin
nonfimbrial adhesion
Country: Inglaterra
Editor: Pergamon-elsevier Science Ltd
Rights: fechado
Identifier DOI: 10.1016/j.cimid.2006.08.003
Date Issue: 2006
Appears in Collections:Unicamp - Artigos e Outros Documentos

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