ArticleAntonie van Leeuwenhoek
Domain analysis of lipoprotein LppQ in Mycoplasma mycoides subsp. mycoides SC.
Article in Antonie van Leeuwenhoek. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Protein-specific analysis of humoral immune responses in a clinical trial for vaccines against contagious bovine pleuropneumonia.Clinical and vaccine immunology : CVI · 2010Trial
- Evidence for the Cytoplasmic Localization of the L-α-Glycerophosphate Oxidase in Members of the "Frontiers in microbiology · 2019Article
- Detection of Mycoplasma mycoides subsp. mycoides SC in bronchoalveolar lavage fluids of cows based on a TaqMan real-time PCR discriminating wild type strains from an lppQ(-) mutant vaccine strain used for DIVA-strategies.Journal of microbiological methods · 2010Article
- Multiplex screening of surface proteins from Mycoplasma mycoides subsp. mycoides small colony for an antigen cocktail enzyme-linked immunosorbent assay.Clinical and vaccine immunology : CVI · 2009Article
- Identification of genes coding for B cell antigens of Mycoplasma mycoides subsp. mycoides Small Colony (MmmSC) by using phage display.BMC microbiology · 2009Article
- Unmarked insertional mutagenesis in the bovine pathogen Mycoplasma mycoides subsp. mycoides SC: characterization of a lppQ mutant.Microbiology (Reading, England) · 2008Article
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Authors and funding
6 authors.
Funding
Abstract
The lipoprotein LppQ is the most prominent antigen of Mycoplasma mycoides subsp. mycoides small colony type (SC) during infection of cattle. This pathogen causes contagious bovine pleuropneumonia (CBPP), a devastating disease of considerable socio-economic importance in many countries worldwide. The dominant antigenicity and high specificity for M. mycoides subsp. mycoides SC of lipoprotein LppQ have been exploited for serological diagnosis and for epidemiological investigations of CBPP. Scanning electron microscopy and immunogold labelling were used to provide ultrastructural evidence that LppQ is located to the cell membrane at the outer surface of M. mycoides subsp. mycoides SC. The selectivity and specificity of this method were demonstrated through discriminating localization of extracellular (i.e., in the zone of contact with host cells) vs. integral membrane domains of LppQ. Thus, our findings support the suggestion that the accessible N-terminal domain of LppQ is surface exposed and such surface localization may be implicated in the pathogenesis of CBPP.
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