Variable Surface Glycoprotein from Trypanosoma brucei Undergoes Cleavage by Matrix Metalloproteinases: An in silico Approach
| Autor: | Cláudia Jassica Gonçalves Moreno, Marcelo Silva, Taffarel Melo Torres |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Microbiology (medical) Gelatinases In silico lcsh:Medicine Matrix metalloproteinase Trypanosoma brucei Cleavage (embryo) 03 medical and health sciences variable surface glycoproteins 0302 clinical medicine parasitic diseases Consensus sequence Immunology and Allergy phospholipase C African trypanosomiasis Molecular Biology major surface protein General Immunology and Microbiology Phospholipase C biology Chemistry Communication lcsh:R matrix metalloproteinases Variable surface glycoprotein biology.organism_classification Cell biology 030104 developmental biology Infectious Diseases trypanosoma brucei 030217 neurology & neurosurgery |
| Zdroj: | Pathogens Pathogens, Vol 8, Iss 4, p 178 (2019) |
| ISSN: | 2076-0817 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|