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Variable Surface Glycoprotein from Trypanosoma brucei Undergoes Cleavage by Matrix Metalloproteinases: An in silico Approach

1
Programa de Pós-graduação em Bioquímica, Centro de Biociências, Universidade Federal do Rio Grande do Norte, Natal 59012-570, Brazil
2
Centro de Ciências Biológicas e da Saúde- Universidade Federal Rural de Semi-árido, Mossoró 59625-900, Brazil
3
Departamento de Análises Clínicas e Toxicológicas, Centro de Ciências da Saúde, Universidade Federal do Rio Grande do Norte, Natal 59012-570, Brazil
4
Global Health and Tropical Medicine, Instituto de Higiene e Medicina Tropical, Universidade Nova de Lisboa, 1800-166 Lisbon, Portugal
*
Author to whom correspondence should be addressed.
Pathogens 2019, 8(4), 178; https://doi.org/10.3390/pathogens8040178
Received: 30 July 2019 / Revised: 24 September 2019 / Accepted: 25 September 2019 / Published: 8 October 2019
(This article belongs to the Section Human Pathogens)
In order to survive as extracellular parasites in the mammalian host environment, Trypanosoma brucei has developed efficient mechanisms of immune system evasion, which include the abundant expression of a variable surface glycoprotein (VSG) coat. VSGs are anchored in the parasite membrane by covalent C-terminal binding to glycosylphosphatidylinositol and may be periodically removed by a phospholipase C (PLC) and a major surface protein (TbMSP). VSG molecules show extraordinary antigenic diversity and a comparative analysis of protein sequences suggests that conserved elements may be a suitable target against African trypanosomiasis. However, the cleavage mechanisms of these molecules remain unclear. Moreover, in protozoan infections, including those caused by Trypanosoma brucei, it is possible to observe an increased expression of the matrix metalloproteinases (MMPs). To address the cleavage mechanism of VSGs, the PROSPER server was used for the identification of VSG sequence cleavage sites. After data compilation, it was observed that 64 VSG consensus sequences showed a high conservation of hydrophobic residues, such as valine (V), methionine (M), leucine (L) and isoleucine (I) in the fifth position—the exact location of the cleavage site. In addition, the PROSPER server identified conserved cleavage site portions of VSG proteins recognized by three matrix metalloproteases (gelatinases: MMP-2, MMP-3 and MMP-9). However, further biological studies are needed in order to analyze and confirm this prediction. View Full-Text
Keywords: variable surface glycoproteins; phospholipase C; matrix metalloproteinases; major surface protein; Trypanosoma brucei; African trypanosomiasis variable surface glycoproteins; phospholipase C; matrix metalloproteinases; major surface protein; Trypanosoma brucei; African trypanosomiasis
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Moreno, C.J.G.; Torres, T.; Silva, M.S. Variable Surface Glycoprotein from Trypanosoma brucei Undergoes Cleavage by Matrix Metalloproteinases: An in silico Approach. Pathogens 2019, 8, 178.

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