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Publication Abstract from PubMed

The 57-residue small hydrophilic endoplasmic reticulum-associated protein (SHERP) shows highly specific, stage-regulated expression in the non-replicative vector-transmitted stages of the kinetoplastid parasite, Leishmania major, the causative agent of human cutaneous leishmaniasis. Previous studies have demonstrated that SHERP localises as a peripheral membrane protein on the cytosolic face of the endoplasmic reticulum and on outer mitochondrial membranes while its high copy number suggests a critical function in vivo. However, the absence of defined domains or identifiable orthologues, together with lack of a clear phenotype in transgenic parasites lacking SHERP, has limited functional understanding of this protein. Here, we use a combination of biophysical and biochemical methods to demonstrate that SHERP can be induced to adopt a globular fold in the presence of anionic lipids or sodium dodecyl sulfate. Crosslinking and binding studies suggest that SHERP has the potential to form a complex with the vacuolar type H+-ATPase. Taken together, these results suggest that SHERP may function in modulating cellular processes related to membrane organization and/or acidification during vector transmission of infective Leishmania.

Structural basis of molecular recognition the Leishmania small hydrophillic endoplasmic reticulum-associated protein, SHERP, at membrane surfaces.,Moore B, Miles AJ, Guerra-Giraldez C, Simpson PJ, Iwata M, Wallace BA, Matthews SJ, Smith DF, Brown KA J Biol Chem. 2010 Nov 24. PMID:21106528^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.