Bonvin, Laetitia Anne; Vilei, Edy M.; Kühni Boghenbor, Kathrin; Kapp, Nadine; Frey, Joachim; Stoffel, Michael Hubert (2008). Domain analysis of lipoprotein LppQ in Mycoplasma mycoides subsp. mycoides SC. Antonie van Leeuwenhoek - international journal of general and molecular microbiology, 93(1-2), pp. 175-183. Dordrecht: Springer Netherlands 10.1007/s10482-007-9191-1
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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.
Item Type: |
Journal Article (Original Article) |
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Division/Institute: |
05 Veterinary Medicine > Department of Infectious Diseases and Pathobiology (DIP) > Institute of Veterinary Bacteriology 05 Veterinary Medicine > Department of Clinical Research and Veterinary Public Health (DCR-VPH) > Veterinary Anatomy |
UniBE Contributor: |
Bonvin, Laetitia Anne, Vilei, Edi, Kühni, Kathrin, Kapp, Nadine, Frey, Joachim, Stoffel, Michael Hubert |
Subjects: |
600 Technology > 630 Agriculture 500 Science > 570 Life sciences; biology |
ISSN: |
0003-6072 |
Publisher: |
Springer Netherlands |
Language: |
English |
Submitter: |
Factscience Import |
Date Deposited: |
04 Oct 2013 15:24 |
Last Modified: |
02 Mar 2023 23:23 |
Publisher DOI: |
10.1007/s10482-007-9191-1 |
Web of Science ID: |
000251648200016 |
BORIS DOI: |
10.7892/boris.37769 |
URI: |
https://boris.unibe.ch/id/eprint/37769 (FactScience: 210655) |