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cDNA cloning, expression and characterization of a Boophilus microplus paramyosin

Published online by Cambridge University Press:  16 January 2003

C. A. S. FERREIRA
Affiliation:
Centro de Biotecnologia do Estado do Rio Grande do Sul, Porto Alegre, RS, Brazil – C.P. 15005 – CEP 91501-970 Departamento de Ciências Microbiológicas, PUC-RS, Av. Ipiranga 6681, Porto Alegre, RS, Brazil – CEP 90619-900 Centro de Ciências da Saúde, UNISINOS, Av. Unisinos 950, São Leopoldo, RS, Brazil – CEP 93022-000
M. C. BARBOSA
Affiliation:
Centro de Biotecnologia do Estado do Rio Grande do Sul, Porto Alegre, RS, Brazil – C.P. 15005 – CEP 91501-970
T. C. L. SILVEIRA
Affiliation:
Centro de Biotecnologia do Estado do Rio Grande do Sul, Porto Alegre, RS, Brazil – C.P. 15005 – CEP 91501-970
J. G. VALENZUELA
Affiliation:
Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 4 Center Dr., Rm. 4/126, Bethesda, MD 20892, USA
I. DA SILVA VAZ JR
Affiliation:
Centro de Biotecnologia do Estado do Rio Grande do Sul, Porto Alegre, RS, Brazil – C.P. 15005 – CEP 91501-970 Departamento de Biologia Molecular e Biotecnologia, Porto Alegre, RS, Brazil – C.P. 15005 – CEP 91501-970 Faculdade de Veterinária, UFRGS, Av. Bento Gonçalves 9500, Porto Alegre, RS, Brazil – C.P. 15005 – CEP 91501-970
A. MASUDA
Affiliation:
Centro de Biotecnologia do Estado do Rio Grande do Sul, Porto Alegre, RS, Brazil – C.P. 15005 – CEP 91501-970 Departamento de Biologia Molecular e Biotecnologia, Porto Alegre, RS, Brazil – C.P. 15005 – CEP 91501-970

Abstract

The tick Boophilus microplus is a 1-host tick that causes important losses to bovine herds, and protective antigens are being investigated in order to develop vaccines that avoid the use of acaricides. Paramyosins are multi-functional invertebrate muscle proteins, whose roles may include host immunomodulation, and seem to be a prominent candidate in a schistosomiasis vaccine. We report here the cloning, expression and characterization of a B. microplus paramyosin (BmPRM). Sequence analysis of the full length coding sequence cDNA shows high identity to other arthropod paramyosin sequences, and the predicted molecular weight, pI and secondary structure are consistent with a typical paramyosin. Western-blot expression analysis indicates the presence of BmPRM in all tissues and developmental stages tested, but not in saliva. The recombinant protein (rBmPRM) was shown to bind both IgG and collagen. Possible implications of these activities with host evasion mechanisms are discussed.

Type
Research Article
Copyright
© 2002 Cambridge University Press

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