Identification of potential protein partners that bind to the variant surface glycoprotein in Trypanosoma equiperdum
| Autor: | José L. Escalona, José Bubis, Liomary M. Carrasquel, Alvaro Acosta-Serrano, Yurong Guo |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Alanine chemistry.chemical_classification Trypanosoma 030102 biochemistry & molecular biology biology Protozoan Proteins Trypanosoma brucei biology.organism_classification Molecular biology Protein–protein interaction Gene product 03 medical and health sciences 030104 developmental biology Infectious Diseases chemistry parasitic diseases Antigenic variation Trypanosoma equiperdum Animal Science and Zoology Parasitology Glycoprotein Variant Surface Glycoproteins Trypanosoma Protein Binding |
| Zdroj: | Parasitology. 144(7) |
| ISSN: | 1469-8161 |
| Popis: | SUMMARYTrypanosoma equiperdumpossesses a dense coat of a variant surface glycoprotein (VSG) that is used to evade the host immune response by a process known as antigenic variation. Soluble and membrane forms of the predominant VSG from the VenezuelanT. equiperdumTeAp-N/D1 strain (sVSG and mVSG, respectively) were purified to homogeneity; and antibodies against sVSG and mVSG were raised, isolated, and employed to produce anti-idiotypic antibodies that structurally mimic the VSG surface. Prospective VSG-binding partners were initially detected by far-Western blots, and then by immunoblots using the generated anti-idiotypic antibodies. Polypeptides of ~80 and 55 kDa were isolated when anti-idiotypic antibodies–Sepharose affinity matrixes were used as baits. Mass spectrometry sequencing yielded hits with various proteins fromTrypanosoma bruceisuch as heat-shock protein 70, tryparedoxin peroxidase, VSG variants, expression site associated gene product 6, and two hypothetical proteins. In addition, a possible interaction with a protein homologous to the glutamic acid/alanine-rich protein fromTrypanosoma congolensewas also found. These results indicate that the corresponding orthologous gene products are candidates for VSG-interacting proteins inT. equiperdum. |
| Databáze: | OpenAIRE |
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