ArticleThe Biochemical journal2001
Characterization of a differentially expressed protein that shows an unusual localization to intracellular membranes in Leishmania major.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 53 citations in OpenAlex.
- Detection of Leishmania metacyclogenesis within the sand fly vector employing a real-time PCR for sherp gene expression: A tool for Leishmania surveillance and transmission potential.PLoS neglected tropical diseases · 2025Article
- Single-cell atlas ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- CYP5122A1 encodes an essential sterol C4-methyl oxidase in Leishmania donovani and determines the antileishmanial activity of antifungal azoles.Nature communications · 2024Article
- TORC1 is an essential regulator of nutrient-controlled proliferation and differentiation in Leishmania.EMBO reports · 2024Article
- Article
- High-speed, three-dimensional imaging reveals chemotactic behaviour specific to human-infectiveeLife · 2021Article
- Identifying miltefosine-resistant key genes in protein-protein interactions network and experimental verification in Iranian Leishmania major.Molecular biology reports · 2019Article
- QuantifyingCommunications biology · 2019Article
- Genomic and transcriptomic alterations in Leishmania donovani lines experimentally resistant to antileishmanial drugs.International journal for parasitology. Drugs and drug resistance · 2018Article
- Leishmania HASP and SHERP Genes Are Required for In Vivo Differentiation, Parasite Transmission and Virulence Attenuation in the Host.PLoS pathogens · 2017Article
- Genomic Appraisal of the Multifactorial Basis for In Vitro Acquisition of Miltefosine Resistance in Leishmania donovani.Antimicrobial agents and chemotherapy · 2016Article
- Transcriptomic profiling of gene expression and RNA processing during Leishmania major differentiation.Nucleic acids research · 2015Article
- Fitness and Phenotypic Characterization of Miltefosine-Resistant Leishmania major.PLoS neglected tropical diseases · 2015Article
- Comparative transcript expression analysis of miltefosine-sensitive and miltefosine-resistant Leishmania donovani.Parasitology research · 2014Article
- The Leishmania major BBSome subunit BBS1 is essential for parasite virulence in the mammalian host.Molecular microbiology · 2013Article
- Impact of continuous axenic cultivation in Leishmania infantum virulence.PLoS neglected tropical diseases · 2012Article
- Structural basis of molecular recognition of the Leishmania small hydrophilic endoplasmic reticulum-associated protein (SHERP) at membrane surfaces.The Journal of biological chemistry · 2011Article
- The stage-regulated HASPB and SHERP proteins are essential for differentiation of the protozoan parasite Leishmania major in its sand fly vector, Phlebotomus papatasi.Cellular microbiology · 2010Article
- Leishmania-specific surface antigens show sub-genus sequence variation and immune recognition.PLoS neglected tropical diseases · 2010Article
- Leishmania dihydroxyacetonephosphate acyltransferase LmDAT is important for ether lipid biosynthesis but not for the integrity of detergent resistant membranes.Molecular and biochemical parasitology · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The SHERP genes are found as a tandem pair within the differentially regulated LmcDNA16 locus of Leishmania major. The SHERP gene product (small hydrophilic endoplasmic reticulum-associated protein) is unusual in its small size (6.2 kDa), its acidic pI (4.6) and its exclusive, high-level expression ( approximately 100000 copies per cell) in infective non-replicative parasite stages. No homologues have been found to date. Secondary-structure predictions suggest that SHERP contains an amphiphilic alpha-helix that is presumably involved in protein-protein interactions. SHERP has been localized to the endoplasmic reticulum as well as to the outer mitochondrial membrane in both wild-type and over-expressing parasites. Given the absence of an N-terminal signal sequence, transmembrane-spanning domains or detectable post-translational modifications, it is likely that this hydrophilic molecule is a peripheral membrane protein on the cytosolic face of intracellular membranes. This weak membrane association has been confirmed in cell-fractionation assays, in which SHERP redistributes from the cytoplasmic to the membrane fraction after in vivo cross-linking. SHERP does not appear to be involved in rearrangements of the cytoskeleton or conservation of organelle morphology during parasite differentiation. The role of this novel protein, presumed to be part of a protein complex, in infective parasites that are nutrient-deficient and pre-adapted for intracellular survival in the mammalian host is under investigation.
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