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Identification of potential protein partners that bind to the variant surface glycoprotein in Trypanosoma equiperdum

Published online by Cambridge University Press:  10 February 2017

LIOMARY M. CARRASQUEL ,
JOSÉ L. ESCALONA ,
ALVARO ACOSTA-SERRANO ,
YURONG GUO  and
JOSÉ BUBIS Open the ORCID record for JOSÉ BUBIS [Opens in a new window]
LIOMARY M. CARRASQUEL
Affiliation:
Departamento de Biología Celular, Universidad Simón Bolívar, Caracas, Venezuela
JOSÉ L. ESCALONA
Affiliation:
Departamento de Biología Celular, Universidad Simón Bolívar, Caracas, Venezuela Postgrado en Química, Universidad Simón Bolívar, Caracas, Venezuela
ALVARO ACOSTA-SERRANO
Affiliation:
Parasitology Department, Liverpool School of Tropical Medicine, Liverpool, UK
YURONG GUO
Affiliation:
Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, California 92093-0654, USA
JOSÉ BUBIS*
Affiliation:
Departamento de Biología Celular, Universidad Simón Bolívar, Caracas, Venezuela
*
*Corresponding author: Laboratorio de Química de Proteínas, Departamento de Biología Celular, Universidad Simón Bolívar, Apartado 89·000, Valle de Sartenejas, Baruta, Caracas 1081-A, Venezuela. E-mail: jbubis@usb.ve
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Summary

Trypanosoma equiperdum possesses 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 Venezuelan T. equiperdum TeAp-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 from Trypanosoma brucei such 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 from Trypanosoma congolense was also found. These results indicate that the corresponding orthologous gene products are candidates for VSG-interacting proteins in T. equiperdum.

Keywords

Trypanosoma equiperdumvariant surface glycoproteinglycosylphosphatidylinositol-anchored proteinsanti-idiotypic antibodiesprotein–protein interactions
Type
Research Article
Information
Parasitology , Volume 144 , Issue 7 , June 2017 , pp. 923 - 936
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Copyright
Copyright © Cambridge University Press 2017 

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Footnotes

‡

Present address: Sorrento Therapeutics Inc., 9380 Judicial Drive, San Diego, California 92121, USA.

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