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

被引：17

作者：

CLEAVINGER, CM ^{[1
]}

KIM, MF ^{[1
]}

WISE, KS ^{[1
]}

机构：

[1] UNIV MISSOURI,DEPT MOLEC MICROBIOL & IMMUNOL,COLUMBIA,MO 65212

来源：

JOURNAL OF BACTERIOLOGY | 1994年 / 176卷 / 08期

关键词：

D O I：

10.1128/JB.176.8.2463-2467.1994

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：2463 / 2467

页数：5

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