cDNA cloning, expression and characterization of a Boophilus microplus paramyosin

被引:20
作者
Ferreira, CAS
Barbosa, MC
Silveira, TCL
Valenzuela, JG
Vaz, ID
Masuda, A
机构
[1] Univ Fed Rio Grande do Sul, Ctr Biotecnol Estado Rio Grande Sul, BR-91501970 Porto Alegre, RS, Brazil
[2] Univ Fed Rio Grande do Sul, Dept Biol Mol & Biotecnol, BR-91501970 Porto Alegre, RS, Brazil
[3] Univ Fed Rio Grande do Sul, Fac Vet, BR-91501970 Porto Alegre, RS, Brazil
[4] NIAID, Parasit Dis Lab, NIH, Bethesda, MD 20892 USA
[5] PUC RS, Dept Ciencias Microbiol, BR-90619900 Porto Alegre, RS, Brazil
[6] Univ Vale Rio dos Sinos, Ctr Ciencias Saude, BR-93022000 Sao Leopoldo, RS, Brazil
关键词
paramyosin; Boophilus microplus; IgG binding protein; collagen binding protein; tick;
D O I
10.1017/S0031182002002019
中图分类号
R38 [医学寄生虫学]; Q [生物科学];
学科分类号
07 ; 0710 ; 09 ; 100103 ;
摘要
The tick Boophilus microphis is a I-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. nacroplus 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.
引用
收藏
页码:265 / 274
页数:10
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