Abstract
Antiserum and purified immunoglobulin directed against Mycoplasma pneumoniae membrane protein P1 were examined for their influence on mycoplasma viability, metabolism, and cytadsorption. Anti-P1 immunoglobulin inhibited adherence of M. pneumoniae to hamster tracheal rings in vitro by up to 80% and inhibited hemadsorption by greater than 90%. Cytadsorption was also inhibited by anti-P1 Fab fragments. Anti-P1 antibodies had no effect on M. pneumoniae viability or metabolism. The data indicate that anti-P1 antibody obstructs the interaction of M. pneumoniae adhesin P1 with its host receptors.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1180-1186 |
| Number of pages | 7 |
| Journal | Infection and Immunity |
| Volume | 39 |
| Issue number | 3 |
| State | Published - 1983 |
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ASJC Scopus subject areas
- Immunology
Cite this
Inhibition of Mycoplasma pneumoniae hemadsorption and adherence to respiratory epithelium by antibodies to a membrane protein. / Krause, D. C.; Baseman, J. B.
In: Infection and Immunity, Vol. 39, No. 3, 1983, p. 1180-1186.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Inhibition of Mycoplasma pneumoniae hemadsorption and adherence to respiratory epithelium by antibodies to a membrane protein
AU - Krause, D. C.
AU - Baseman, J. B.
PY - 1983
Y1 - 1983
N2 - Antiserum and purified immunoglobulin directed against Mycoplasma pneumoniae membrane protein P1 were examined for their influence on mycoplasma viability, metabolism, and cytadsorption. Anti-P1 immunoglobulin inhibited adherence of M. pneumoniae to hamster tracheal rings in vitro by up to 80% and inhibited hemadsorption by greater than 90%. Cytadsorption was also inhibited by anti-P1 Fab fragments. Anti-P1 antibodies had no effect on M. pneumoniae viability or metabolism. The data indicate that anti-P1 antibody obstructs the interaction of M. pneumoniae adhesin P1 with its host receptors.
AB - Antiserum and purified immunoglobulin directed against Mycoplasma pneumoniae membrane protein P1 were examined for their influence on mycoplasma viability, metabolism, and cytadsorption. Anti-P1 immunoglobulin inhibited adherence of M. pneumoniae to hamster tracheal rings in vitro by up to 80% and inhibited hemadsorption by greater than 90%. Cytadsorption was also inhibited by anti-P1 Fab fragments. Anti-P1 antibodies had no effect on M. pneumoniae viability or metabolism. The data indicate that anti-P1 antibody obstructs the interaction of M. pneumoniae adhesin P1 with its host receptors.
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UR - http://www.scopus.com/inward/citedby.url?scp=0020691316&partnerID=8YFLogxK
M3 - Article
C2 - 6404820
AN - SCOPUS:0020691316
VL - 39
SP - 1180
EP - 1186
JO - Infection and Immunity
JF - Infection and Immunity
SN - 0019-9567
IS - 3
ER -