PROCESSING AND SURFACE PRESENTATION OF THE MYCOPLASMA-HYORHINIS VARIANT LIPOPROTEIN VLPC

The variant surface lipoprotein VlpC of Mycoplasma hyorhinis was shown to be processed by cleavage of a characteristic prokaryotic prolipopr otein signal peptide. In addition, a vlpC::phoA fusion protein express ed and translocated in Escherichia coli was recognized by surface-bind ing monoclonal antibodies, which identified the characteristic region II of Vlps, containing divergent external sequences proximal to the me mbrane, as an exposed portion of these surface proteins subject to imm une recognition and selection.