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Characterization of a nonfimbrial mannose-sensitive hemagglutinin (MSH) produced by Salmonella enterica serovar enteritidis |
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| Authors: | Mikcha Jane M G Freire Maria G Macedo Maria Ligia R Yano Tomomasa Piantino Ferreira Antonio J |
| Institution: | aDepartamento de Análises Clínicas, Universidade Estadual de Maringá, Paraná, Brazil bDepartamento de Bioquímica, Instituto de Biologia, Universidade Estadual de Campinas, São Paulo, Brazil cDepartamento de Microbiologia e Imunologia, Instituto de Biologia, Universidade Estadual de Campinas, São Paulo, Brazil dDepartamento de Patologia, Faculdade de Medicina Veterinária e Zootecnia, Universidade de São Paulo, Av. Prof. Dr. Orlando Marques de Paiva, 87, São Paulo, SP Cep: 05508-900, Brazil |
| 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 40 kDa 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. |
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