Investigation of lectin activity in Theileria annulata piroplasms

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dc.authoridKarapinar, Tolga/0000-0003-1724-491X
dc.authorwosidGüldür, Tayfun/AAA-7088-2021
dc.authorwosidKarapinar, Tolga/W-3858-2018
dc.contributor.authorKaynar, Ö
dc.contributor.authorGüldür, T
dc.contributor.authorKarapinar, T
dc.date.accessioned2024-08-04T20:13:46Z
dc.date.available2024-08-04T20:13:46Z
dc.date.issued2005
dc.departmentİnönü Üniversitesien_US
dc.description.abstractAdhesion to target cells is an essential step in the pathogenesis of many protozoal infections. Some protozoa have been reported to have a lectin activity involved in their attachment to the cell surface. The ligand-receptor interaction involved in Theileria annulata infection is unclear at present, in spite of the fact that some aspects of the process have been investigated. To this end, T annulata piroplasms have been screened for lectin activity. Blood taken from infected cattle was first depleted of leukocytes and then subjected to ammonium chloride lysis in order to isolate the piroplasms. The piroplasms were homogenised and a crude membrane extract was prepared by centrifugation. To investigate lectin activity in piroplasm proteins, a simple screening procedure was employed for analysing piroplasm proteins binding to various lectin ligands. Numerous immobilised lectin ligands (L-fucose-sepharose, N-acetyl-neuraminic acid-sepharose, N-acetyl-D-galactosamine-agarose, N-acetyl-D-glucosamine-agarose, D-mannose-agarose, beta-D-glucose-agarose, a-methyl-D-mannoside-agarose) were incubated with T annulata piroplasm crude membrane extract. The ligand-bound proteins were eluted and separated by a brief centrifugation and determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The present study suggests that a 32 kDa protein of piroplasm binds to D-galactosyl residues of the agarose matrix and that the binding is inhibited by galactose and not by the other monosaccharides tested.en_US
dc.identifier.doi10.1556/AVet.53.2005.1.6
dc.identifier.endpage63en_US
dc.identifier.issn0236-6290
dc.identifier.issn1588-2705
dc.identifier.issue1en_US
dc.identifier.pmid15782659en_US
dc.identifier.scopus2-s2.0-14644391424en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage53en_US
dc.identifier.urihttps://doi.org/10.1556/AVet.53.2005.1.6
dc.identifier.urihttps://hdl.handle.net/11616/93827
dc.identifier.volume53en_US
dc.identifier.wosWOS:000227624500006en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherAkademiai Kiado Zrten_US
dc.relation.ispartofActa Veterinaria Hungaricaen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectTheileria annulataen_US
dc.subjectpiroplasmen_US
dc.subjectgal-lectinen_US
dc.titleInvestigation of lectin activity in Theileria annulata piroplasmsen_US
dc.typeArticleen_US

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