TY - JOUR
T1 - Detection of mip-like sequences and mip-related proteins within the family Rickettsiaceae
AU - Cianciotto, Nicholas P.
AU - O'Connell, William
AU - Dasch, Gregory A.
AU - Mallavia, Louis P.
PY - 1995/3
Y1 - 1995/3
N2 - The Mip surface protein, a prokaryotic analog of the FK506-binding proteins, enhances the ability of Legionella pneumophila to infect macrophages and protozoa. Using mip-specific probes and low-stringency Southern hybridizations, we have detected DNA sequences homologous to mip within Coxiella burnetii and Rochalimaea quintana. Using specific anti-Mip antisera and immunoblot analysis, we also detected Mip-related proteins within these bacteria as well as within Rickettsia and Ehrlichia species. These data suggest that Mip-related proteins have broad significance for host-parasite interactions. However, they also indicate that care must be exercised when using mip probes or anti-Mip antibodies for the detection of Legionella organisms in water or clinical samples.
AB - The Mip surface protein, a prokaryotic analog of the FK506-binding proteins, enhances the ability of Legionella pneumophila to infect macrophages and protozoa. Using mip-specific probes and low-stringency Southern hybridizations, we have detected DNA sequences homologous to mip within Coxiella burnetii and Rochalimaea quintana. Using specific anti-Mip antisera and immunoblot analysis, we also detected Mip-related proteins within these bacteria as well as within Rickettsia and Ehrlichia species. These data suggest that Mip-related proteins have broad significance for host-parasite interactions. However, they also indicate that care must be exercised when using mip probes or anti-Mip antibodies for the detection of Legionella organisms in water or clinical samples.
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U2 - 10.1007/BF00296200
DO - 10.1007/BF00296200
M3 - Article
C2 - 7532505
AN - SCOPUS:0028934899
SN - 0343-8651
VL - 30
SP - 149
EP - 153
JO - Current Microbiology
JF - Current Microbiology
IS - 3
ER -