作者: Jane M.G. Mikcha , Maria G. Freire , Maria Ligia R. Macedo , Tomomasa Yano , Antonio J. Piantino Ferreira
DOI: 10.1016/J.CIMID.2006.08.003
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摘要: Abstract A nonfimbrial mannose-sensitive hemagglutinin (MSH) with adhesive properties produced by Salmonella enterica serovar Enteritidis was characterized. The MSH characterized as glycoprotein and consisted of three noncovalently bound subunits M r 28, 33 40 kDa determined SDS-PAGE. heat-stable resistant to alkaline (high) or acid (low) pH, however, it inhibited proteolytic enzymes, EDTA sodium periodate. Mouse antiserum raised against reacted the 28 kDa band in immunoblotting, also hemagglutination bacterial adherence HeLa cells. Electron microscope examinations showed that is not a fimbriae-like structure. anti-MSH IgG competitively immunofluorescence test, using on cells specific IgG, supported view contributes organism. These results indicate putative factor may mediate enteritidis eucaryotic