Identification of a thrombospondin-like immunodominant and phosphorylcholine-containing glycoprotein (GP300) in Dictyocaulus viviparus and related nematodes
| Autor: | Kooyman, Frans N J, van Balkom, Bas W M, de Vries, Erik, van Putten, Jos P M, LS Klinisch Onderzoek Wagenaar, LS Virologie, Faculteit Diergeneeskunde, LS Infectiebiologie (Bacteriologie), I&I AVM |
|---|---|
| Přispěvatelé: | LS Klinisch Onderzoek Wagenaar, LS Virologie, Faculteit Diergeneeskunde, LS Infectiebiologie (Bacteriologie), I&I AVM |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Glycan
Protein family medicine.medical_treatment Phosphorylcholine Molecular Sequence Data Biology Mass Spectrometry Genetic Models medicine Helminth Animals Amino Acid Sequence Antigens Molecular Biology Peptide sequence Glycoproteins chemistry.chemical_classification Thrombospondin Protease Models Genetic Helminth Proteins biology.organism_classification Dictyocaulus Molecular Weight chemistry Biochemistry Antigens Helminth Immunology biology.protein Parasitology Glycoprotein Thrombospondins |
| Zdroj: | Molecular and Biochemical Parasitology, 163(2), 85. Elsevier |
| ISSN: | 0166-6851 |
| Popis: | GP300 is a high molecular weight glycoprotein of the bovine lungworm Dictyocaulus viviparus. The N-linked glycans are substituted with phosphorylcholine (PC) giving it immunomodulatory potential. GP300 is highly immunogenic and its recognition by IgE antibodies is correlated with protection against infection. Here we identified and characterized the protein backbone of GP300. Mass spectrometric analysis on purified GP300 and DNA sequencing of the corresponding gene indicated that GP300 is a thrombospondin-like protein with 7 thrombospondin domains, 6 kunitz domains and 15 putative N-glycosylation sites. Purified GP300 display protease inhibitory activity. The protein was located in the brushborder of the gut, but also in muscles, hypodermis and the lining of the uterus. Analysis of GP300 orthologues in Haemonchus contortus and Cooperia oncophora revealed that these proteins also contain PC-substituted N-glycans and showed immunological cross-reactive responses. These data suggest the existence in nematodes of a GP300 protein family that is characterized by PC-substituted N-linked glycans attached to a thrombospondin-like protein backbone. This finding is of particular interest considering the immunomodulatory and vaccine potential of members of the GP300 family. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect