Picture of athlete cycling

Open Access research with a real impact on health...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of Open Access research papers by Strathclyde researchers, including by researchers from the Physical Activity for Health Group based within the School of Psychological Sciences & Health. Research here seeks to better understand how and why physical activity improves health, gain a better understanding of the amount, intensity, and type of physical activity needed for health benefits, and evaluate the effect of interventions to promote physical activity.

Explore open research content by Physical Activity for Health...

Oligopeptidase B deficient mutants of Leishmania major

Munday, Jane C. and McLuskey, Karen and Brown, Elaine and Coombs, Graham H and Mottram, Jeremy C (2011) Oligopeptidase B deficient mutants of Leishmania major. Molecular and Biochemical Parasitology, 175 (1). pp. 49-57. ISSN 0166-6851

Full text not available in this repository. Request a copy from the Strathclyde author

Abstract

Oligopeptidase B is a clan SC, family S9 serine peptidase found in gram positive bacteria, plants and try-panosomatids. Evidence suggests it is a virulence factor and thus therapeutic target in both Trypanosome cruzi and T. brucei, but little is known about its function in Leishmania. In this study L major OPB-deficient mutants (Delta opb) were created. These grew normally as promastigotes, had a small deficiency in their ability to undergo differentiation to metacyclic promastigotes, were significantly less able to infect and survive within macrophages in vitro, but were virulent to mice. These data suggest that L major OPB itself is not an important virulence factor, indicating functional differences between trypanosomes and Leishmania in their interaction with the mammalian host. The possibility that an OPB-like enzyme (designated OPB2) in L major might compensate for the loss of OPB in Delta opb was investigated via by mapping its sequence onto the 1.6 angstrom structure of L. major OPB. This suggested that the residues involved in the S1 and S2 subsites of OPB2 are identical to OPB and hence the substrate specificity would be similar. Consequently there may be redundancy between the two enzymes. (C) 2010 Elsevier B.V. All rights reserved.