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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Antigens, Bacterial*
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism*
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Base Sequence
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Cloning, Molecular
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Epitopes / analysis
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Escherichia coli / metabolism
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Lipoproteins / chemistry
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Lipoproteins / metabolism*
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Molecular Sequence Data
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Mycoplasma / chemistry
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Mycoplasma / metabolism*
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Protein Sorting Signals / metabolism*
Substances
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Antigens, Bacterial
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Bacterial Proteins
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Epitopes
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Lipoproteins
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Protein Sorting Signals
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VlpC protein, Mycoplasma hyorhinis