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. 1994 Apr;176(8):2463–2467. doi: 10.1128/jb.176.8.2463-2467.1994

Processing and surface presentation of the Mycoplasma hyorhinis variant lipoprotein VlpC.

C M Cleavinger 1, M F Kim 1, K S Wise 1
PMCID: PMC205375  PMID: 7512554

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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