Processing and surface presentation of the Mycoplasma hyorhinis variant lipoprotein VlpC.
AUTOR(ES)
Cleavinger, C M
RESUMO
The variant surface lipoprotein VlpC of Mycoplasma hyorhinis was shown to be processed by cleavage of a characteristic prokaryotic prolipoprotein signal peptide. In addition, a vlpC::phoA fusion protein expressed and translocated in Escherichia coli was recognized by surface-binding monoclonal antibodies, which identified the characteristic region II of Vlps, containing divergent external sequences proximal to the membrane, as an exposed portion of these surface proteins subject to immune recognition and selection.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=205375Documentos Relacionados
- The Vlp system of Mycoplasma hyorhinis: combinatorial expression of distinct size variant lipoproteins generating high-frequency surface antigenic variation.
- Elongated versions of Vlp surface lipoproteins protect Mycoplasma hyorhinis escape variants from growth-inhibiting host antibodies.
- Increased structural and combinatorial diversity in an extended family of genes encoding Vlp surface proteins of Mycoplasma hyorhinis.
- A family of phase- and size-variant membrane surface lipoprotein antigens (Vsps) of Mycoplasma bovis.
- Gene Families Encoding Phase- and Size-Variable Surface Lipoproteins of Mycoplasma hyorhinis