دورية أكاديمية
Glycosylation of gp116 and gp64 envelope proteins of yellow head virus of Penaeus monodon shrimp.
| العنوان: | Glycosylation of gp116 and gp64 envelope proteins of yellow head virus of Penaeus monodon shrimp. |
|---|---|
| المؤلفون: | Soowannayan C; CSIRO Livestock Industries, Queensland Bioscience Precinct, St Lucia, QLD 4067, Australia. chumporn@biotec.or.th, Cowley JA, Pearson RD, Wallis TP, Gorman JJ, Michalski WP, Walker PJ |
| المصدر: | The Journal of general virology [J Gen Virol] 2010 Oct; Vol. 91 (Pt 10), pp. 2463-73. Date of Electronic Publication: 2010 Jun 16. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Microbiology Society Country of Publication: England NLM ID: 0077340 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1465-2099 (Electronic) Linking ISSN: 00221317 NLM ISO Abbreviation: J Gen Virol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2015- : London : Microbiology Society Original Publication: London, Cambridge Univ. Press for the Society for General Microbiology. |
| مواضيع طبية MeSH: | Protein Processing, Post-Translational*, Penaeidae/*virology , Roniviridae/*physiology , Viral Envelope Proteins/*metabolism, Amino Acid Sequence ; Animals ; Electrophoresis, Polyacrylamide Gel ; Glycosylation ; Mass Spectrometry ; Molecular Sequence Data ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase/metabolism ; Roniviridae/chemistry ; Staining and Labeling/methods ; Viral Envelope Proteins/isolation & purification |
| مستخلص: | Yellow head virus (YHV) is a highly virulent pathogen of Penaeus monodon shrimp that is classified in the genus Okavirus, family Roniviridae, in the order Nidovirales. Separation of virion proteins treated with peptide-N-glycosidase-F (PNGase-F) in SDS-polyacrylamide gels and the use of glycoprotein-specific staining methods indicated that the gp116 and gp64 envelope glycoproteins possess N-linked rather than O-linked glycans. Competitive binding inhibition of lectins with various oligosaccharide specificities indicated that glycans linked to gp64 are mannose-rich, whilst glycans linked to gp116 possess terminal N-acetylgalactosamine and N-acetylglucosamine in addition to terminal mannose-type sugars. Mass spectrometry analyses of peptides generated from YHV proteins before and after deglycosylation with PNGase-F, using combinations of the endoproteinases trypsin, Asp-N and Lys-C, confirmed occupancy of six of the seven potential N-linked glycosylation sites in gp116 and three of the four potential sites in gp64. |
| سلسلة جزيئية: | GENBANK EF156405 |
| المشرفين على المادة: | 0 (Viral Envelope Proteins) EC 3.5.1.52 (Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase) |
| تواريخ الأحداث: | Date Created: 20100618 Date Completed: 20101007 Latest Revision: 20100917 |
| رمز التحديث: | 20240829 |
| DOI: | 10.1099/vir.0.022111-0 |
| PMID: | 20554800 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1465-2099 |
|---|---|
| DOI: | 10.1099/vir.0.022111-0 |