Related Experiment Video
Updated: Jul 19, 2026
Automated Analysis of Intracellular Phenotypes of Salmonella Using ImageJ
Published on: August 9, 2022
Characterization of a nonfimbrial mannose-sensitive hemagglutinin (MSH) produced by Salmonella enterica serovar
Jane M G Mikcha1, Maria G Freire, Maria Ligia R Macedo
1Departamento de Análises Clínicas, Universidade Estadual de Maringá, Paraná, 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 M(r) 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.
Insights
Salmonella Enteritidis produces a nonfimbrial mannose-sensitive hemagglutinin (MSH) that aids bacterial adherence to host cells. This glycoprotein mediates adhesion and is a potential virulence factor for Salmonella Enteritidis infections.
Area of Science:
- Microbiology
- Molecular Biology
- Immunology
Background:
- Salmonella enterica serovar Enteritidis is a significant foodborne pathogen.
- Bacterial adherence to eukaryotic cells is a crucial step in pathogenesis.
- The specific adhesive factors of Salmonella Enteritidis are not fully elucidated.
Purpose of the Study:
- To characterize a nonfimbrial mannose-sensitive hemagglutinin (MSH) from Salmonella Enteritidis.
- To investigate the role of MSH in bacterial adherence to eukaryotic cells.
- To determine if MSH is a potential virulence factor.
Main Methods:
- Biochemical characterization of MSH (SDS-PAGE, pH stability, enzyme sensitivity).
- Antibody production and characterization (immunoblotting, hemagglutination inhibition, adherence inhibition assays).
- Electron microscopy and immunofluorescence microscopy.
Main Results:
- MSH is a heat-stable glycoprotein composed of 28, 33, and 40 kDa subunits.
- MSH mediates mannose-sensitive hemagglutination and bacterial adherence to HeLa cells.
- MSH is not fimbrial and its activity is inhibited by proteases, EDTA, and sodium periodate.
- Antiserum against MSH inhibited hemagglutination and bacterial adherence, confirming MSH's role.
Conclusions:
- MSH is a nonfimbrial adhesive factor produced by Salmonella Enteritidis.
- MSH contributes to the adherence of Salmonella Enteritidis to eukaryotic cells.
- MSH represents a putative virulence factor for Salmonella Enteritidis.
