Abstract
After the polyprotein precursor of retroviral envelope proteins is proteolytically cleaved, the surface (SU) and transmembrane (TM) subunits remain associated with each other by noncovalent interactions or by disulfide bonds. Disulfide linkages confer a relatively stable association between the SU and TM envelope protein subunits of Rous sarcoma virus and murine leukemia virus. In contrast, the noncovalent association between SU and TM of human immunodeficiency virus leads to significant shedding of SU from the surface of infected cells. The SU and TM proteins of bovine leukemia virus (BLV) initially were reported to be disulfide linked but later were concluded not to be, since TM is often lost during purification of SU protein. Here, we show that SU and TM of BLV do, indeed, associate through disulfide bonds, whether the envelope proteins are overexpressed in transfected cells, are produced in virus-infected cells, or are present in newly produced virions.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2930-2935 |
| Number of pages | 6 |
| Journal | Journal of Virology |
| Volume | 74 |
| Issue number | 6 |
| DOIs | |
| State | Published - 2000 |
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ASJC Scopus subject areas
- Immunology
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The SU and TM envelope protein subunits of bovine leukemia virus are linked by disulfide bonds, both in cells and in virions. / Johnston, Elizabeth R.; Radke, Kathryn.
In: Journal of Virology, Vol. 74, No. 6, 2000, p. 2930-2935.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The SU and TM envelope protein subunits of bovine leukemia virus are linked by disulfide bonds, both in cells and in virions
AU - Johnston, Elizabeth R.
AU - Radke, Kathryn
PY - 2000
Y1 - 2000
N2 - After the polyprotein precursor of retroviral envelope proteins is proteolytically cleaved, the surface (SU) and transmembrane (TM) subunits remain associated with each other by noncovalent interactions or by disulfide bonds. Disulfide linkages confer a relatively stable association between the SU and TM envelope protein subunits of Rous sarcoma virus and murine leukemia virus. In contrast, the noncovalent association between SU and TM of human immunodeficiency virus leads to significant shedding of SU from the surface of infected cells. The SU and TM proteins of bovine leukemia virus (BLV) initially were reported to be disulfide linked but later were concluded not to be, since TM is often lost during purification of SU protein. Here, we show that SU and TM of BLV do, indeed, associate through disulfide bonds, whether the envelope proteins are overexpressed in transfected cells, are produced in virus-infected cells, or are present in newly produced virions.
AB - After the polyprotein precursor of retroviral envelope proteins is proteolytically cleaved, the surface (SU) and transmembrane (TM) subunits remain associated with each other by noncovalent interactions or by disulfide bonds. Disulfide linkages confer a relatively stable association between the SU and TM envelope protein subunits of Rous sarcoma virus and murine leukemia virus. In contrast, the noncovalent association between SU and TM of human immunodeficiency virus leads to significant shedding of SU from the surface of infected cells. The SU and TM proteins of bovine leukemia virus (BLV) initially were reported to be disulfide linked but later were concluded not to be, since TM is often lost during purification of SU protein. Here, we show that SU and TM of BLV do, indeed, associate through disulfide bonds, whether the envelope proteins are overexpressed in transfected cells, are produced in virus-infected cells, or are present in newly produced virions.
UR - http://www.scopus.com/inward/record.url?scp=0034001235&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034001235&partnerID=8YFLogxK
U2 - 10.1128/JVI.74.6.2930-2935.2000
DO - 10.1128/JVI.74.6.2930-2935.2000
M3 - Article
VL - 74
SP - 2930
EP - 2935
JO - Journal of Virology
JF - Journal of Virology
SN - 0022-538X
IS - 6
ER -