BYC, an atypical aspartic endopeptidase from Rhipicephalus (Boophilus) microplus eggs

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dc.contributor.authorNascimento-Silva, Maria Clara L.
dc.contributor.authorLeal, Alexandre T.
dc.contributor.authorDaffre, Sirlei
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.contributor.authorSilva Vaz, Itabajara da
dc.contributor.authorPaiva-Silva, Gabriela de O.
dc.contributor.authorOliveira, Pedro L.
dc.contributor.authorSorgine, Marcos Henrique F.
dc.contributor.institutionUniversidade Federal do Rio de Janeiro (UFRJ)
dc.contributor.institutionUniv Fed Rio Grande do Sul
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T13:49:42Z
dc.date.available2016-01-24T13:49:42Z
dc.date.issued2008-04-01
dc.description.abstractAn aspartic endopeptidase was purified in our laboratory from Rhipicephalus (Boophilus) microplus eggs [Logullo, C., Vaz, I.S., Sorgine, M.H., Paiva-Silva, G.O., Faria, F.S., Zingali, R.B., de Lima, M.F., Abreu, L., Oliveira, E.F., Alves, E.W, Masuda, H., Gonzales, J.C., Masuda, A., and Oliveira, P.L., 1998. Isolation of an aspartic proteinase precursor from the egg of a hard tick, Rhipicephalus (Boophilus) microplus. Parasitology 116, 525-532]. Boophilus yolk cathepsin (BYC) was tested as component of a protective vaccine against the tick, inducing a significant immune response in cattle [da Silva, VI., Jr., Logullo, C., Sorgine, M., Velloso, F.F., Rosa de Lima, M.F., Gonzales, J.C., Masuda, H., Oliveira, P.L., and Masuda, A., 1998. Immunization of bovines with an aspartic proteinase precursor isolated from Rhipicephalus (Boophilus) microplus eggs. Vet. Immunol. Immunopathol. 66,331-341]. in this work, BYC was cloned and its primary sequence showed high similarity with other aspartic endopeptidases. in spite of this similarity, BYC sequence shows many important differences in relation to other aspartic peptidases, the most important being the lack of the second catalytic Asp residue, considered to be essential for the catalysis of this class of endopeptidases. When we determined BYC cleavage specificity by LC-MS, we found out that it presents a preference for hydrophobic residues in P1 and P1' in accordance to most aspartic endopeptidases. Also, when analyzed by circular dicroism, BYC presented high beta sheet content, also a characteristic of aspartic endopeptidases. On the other hand, although both native and recombinant BYC are catalytically active, they present a very low specific activity, what seems to indicate that this peptidase will digest its natural substrate, vitellin, very slowly. We speculate that such a slow Vn degradative process might constitute an important strategy to preserve egg protein content to the hatching larvae. (c) 2007 Elsevier Inc. All rights reserved.en
dc.description.affiliationUniv Fed Rio de Janeiro, Ctr Ciencias Saude, Inst Bioquim Med, BR-21941590 Rio de Janeiro, Brazil
dc.description.affiliationUniv Fed Rio Grande do Sul, Ctr Biotechnol, Porto Alegre, RS, Brazil
dc.description.affiliationUniv São Paulo, Inst Ciencias Biomed, Dept Parasitol, BR-05508 São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Escola Paulista Med, Dept Biofis, São Paulo, Brazil
dc.description.affiliationUnifespUniv São Paulo, Escola Paulista Med, Dept Biofis, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent599-607
dc.identifierhttp://dx.doi.org/10.1016/j.cbpb.2007.12.007
dc.identifier.citationComparative Biochemistry and Physiology B-biochemistry & Molecular Biology. New York: Elsevier B.V., v. 149, n. 4, p. 599-607, 2008.
dc.identifier.doi10.1016/j.cbpb.2007.12.007
dc.identifier.issn1096-4959
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/30557
dc.identifier.wosWOS:000254737200008
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofComparative Biochemistry and Physiology B-biochemistry & Molecular Biology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectRhipicephalus microplusen
dc.subjectaspartic endopeptidasesen
dc.subjectcatalytic mechanismen
dc.subjectvitellin degradationen
dc.titleBYC, an atypical aspartic endopeptidase from Rhipicephalus (Boophilus) microplus eggsen
dc.typeinfo:eu-repo/semantics/article
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