Abstract
Adherence of Salmonella typhimurium to mouse peritoneal macrophages (M0) was monitored using a direct microscopic assay and flow cytometry. Competitive binding studies using wild type lipopolysaccharide and derivatives confirmed a role for this moiety in bacterial adherence. M0 pretreated with 2-deoxy-D-glucose exhibited lower binding activity than did untreated controls, suggesting involvement of either Fc or complement receptors. Preexposing M0 to Fc fragments, however, failed to reduce bacterial binding, thus eliminating a role for Fc receptors in this process. M0 pretreated with neutrophil elastase exhibited a diminished ability to bind S. typhimurium, suggesting involvement of complement receptor 1. Monoclonal antibodies M1/70 and M18/2, specific for epitopes on the α and β chains, respectively, of complement receptor 3, also blocked this adherence. In each case we were unable to eliminate completely bacterial adhesion to M0. Monoclonal antibodies to two additional M0 receptors, Mac-2 and Mac-3, did not block bacterial attachment. These data indicate that multiple mechanisms are involved in the initial adhesion of S. typhimurium to mouse M0.
| Original language | English |
|---|---|
| Pages (from-to) | 83-92 |
| Number of pages | 10 |
| Journal | Zentralblatt fur Bakteriologie |
| Volume | 286 |
| Issue number | 1 |
| Publication status | Published - Jun 1997 |
Fingerprint
ASJC Scopus subject areas
- Immunology
Cite this
Adherence of Salmonella typhimurium to murine peritoneal macrophages is mediated by Lipopolysaccharide and complement receptors. / Al-Bahry, Saif N.; Pistole, Thomas G.
In: Zentralblatt fur Bakteriologie, Vol. 286, No. 1, 06.1997, p. 83-92.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Adherence of Salmonella typhimurium to murine peritoneal macrophages is mediated by Lipopolysaccharide and complement receptors
AU - Al-Bahry, Saif N.
AU - Pistole, Thomas G.
PY - 1997/6
Y1 - 1997/6
N2 - Adherence of Salmonella typhimurium to mouse peritoneal macrophages (M0) was monitored using a direct microscopic assay and flow cytometry. Competitive binding studies using wild type lipopolysaccharide and derivatives confirmed a role for this moiety in bacterial adherence. M0 pretreated with 2-deoxy-D-glucose exhibited lower binding activity than did untreated controls, suggesting involvement of either Fc or complement receptors. Preexposing M0 to Fc fragments, however, failed to reduce bacterial binding, thus eliminating a role for Fc receptors in this process. M0 pretreated with neutrophil elastase exhibited a diminished ability to bind S. typhimurium, suggesting involvement of complement receptor 1. Monoclonal antibodies M1/70 and M18/2, specific for epitopes on the α and β chains, respectively, of complement receptor 3, also blocked this adherence. In each case we were unable to eliminate completely bacterial adhesion to M0. Monoclonal antibodies to two additional M0 receptors, Mac-2 and Mac-3, did not block bacterial attachment. These data indicate that multiple mechanisms are involved in the initial adhesion of S. typhimurium to mouse M0.
AB - Adherence of Salmonella typhimurium to mouse peritoneal macrophages (M0) was monitored using a direct microscopic assay and flow cytometry. Competitive binding studies using wild type lipopolysaccharide and derivatives confirmed a role for this moiety in bacterial adherence. M0 pretreated with 2-deoxy-D-glucose exhibited lower binding activity than did untreated controls, suggesting involvement of either Fc or complement receptors. Preexposing M0 to Fc fragments, however, failed to reduce bacterial binding, thus eliminating a role for Fc receptors in this process. M0 pretreated with neutrophil elastase exhibited a diminished ability to bind S. typhimurium, suggesting involvement of complement receptor 1. Monoclonal antibodies M1/70 and M18/2, specific for epitopes on the α and β chains, respectively, of complement receptor 3, also blocked this adherence. In each case we were unable to eliminate completely bacterial adhesion to M0. Monoclonal antibodies to two additional M0 receptors, Mac-2 and Mac-3, did not block bacterial attachment. These data indicate that multiple mechanisms are involved in the initial adhesion of S. typhimurium to mouse M0.
UR - http://www.scopus.com/inward/record.url?scp=0031170863&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031170863&partnerID=8YFLogxK
M3 - Article
VL - 286
SP - 83
EP - 92
JO - International Journal of Medical Microbiology
JF - International Journal of Medical Microbiology
SN - 1438-4221
IS - 1
ER -