CHARACTERIZATION OF A CORONAVIRUS .2. GLYCOPROTEINS OF VIRAL ENVELOPE - TRYPTIC PEPTIDE ANALYSIS
CHARACTERIZATION OF A CORONAVIRUS .2. GLYCOPROTEINS OF VIRAL ENVELOPE - TRYPTIC PEPTIDE ANALYSIS
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DOI:
10.1016/0042-6822(77)90489-5
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发表时间:
1977-01-01
期刊:
影响因子:
3.7
通讯作者:
HOLMES, KV
中科院分区:
文献类型:
--
作者:
STURMAN, LS;HOLMES, KV
Two species of membrane-associated glycoproteins were identified in the coronavirus virion. They are readily distinguished on the basis of size, radiolabeling characteristics and location in relation to the lipid bilayer. The larger glycoprotein is highly labeled by both radiolabeled fucose and glucosamine. This species is found in 2 forms, GP180 and GP90, with apparent MW of 180,000 and 90,000, respectively. GP180 can be converted to GP90 in vitro by treatment of virions with trypsin. Analysis of tryptic digests of GP90 and GP180 give identical peptide patterns. Based on pronase and bromelain sensitivities, GP180/90 is the only protein which is located entirely external to the viral envelope. It appears to comprise the characteristic long, petal-shaped, peplomers of the virion. The smaller glycoprotein, GP23, has an apparent MW of 23,000 and is labeled by radiolabeled glucosamine but not by fucose. The level of glucosamine-labeling of GP23 is .apprx. 1/10 that of GP180/90. GP23 appears to possess 2 distinct domains: a smaller, carbohydrate containing region which is found outside the viral envelope, and a larger portion, highly labeled by methionine, which is integrally associated with the viral membrane. A new nomenclature is proposed for the 3 major coronavirus structural proteins. The 2 envelope glycoproteins GP23 and GP180/90 are designated E1 and E2, respectively; the inner core protein VP50 is designated N.