Isolation of Mycoplasma pulmonis membranes and identification of surface antigens.
AUTOR(ES)
Horowitz, S A
RESUMO
Labeling of Mycoplasma pulmonis cells by iodination with the Bolton-Hunter reagent was shown to efficiently label membrane-associated proteins without significant loss of viability. Labeled proteins proven to be surface exposed by differential proteolytic digestion were analyzed by autoradiography of two-dimensional polyacrylamide gel electrophoresis (PAGE), and seven labeled major polypeptides were identified. To identify all the membrane-associated antigens, pure membranes were isolated by using the surface-labeled proteins as markers. Analysis of the isolated membranes by autoradiography of both sodium dodecyl sulfate-PAGE and the two-dimensional PAGE indicated that the labeled surface proteins were retained in the pure membranes; by immunoblotting with sera from naturally infected animals, these surface proteins were shown to be the predominant antigens recognized by the host during natural infection.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=260507Documentos Relacionados
- Identification of cross-reactive antigens between Mycoplasma pulmonis and Mycoplasma arthritidis.
- Serum antibody and cellular responses in LEW and F344 rats after immunization with Mycoplasma pulmonis antigens.
- Rapid isolation of monoclonal antibodies specific for cell surface differentiation antigens.
- Identification of atypical mycobacteria by thin-layer chromatography of their surface antigens.
- Protection of rats against Mycoplasma arthritidis-induced arthritis by active and passive immunizations with two surface antigens.