TY - JOUR
T1 - Evidence that HIV-1 gag precursor shares antigenic sites with the major capsid protein of human cytomegalovirus
AU - Gibson, Wade
AU - McNally, Lisa M.
AU - Benveniste, Raoul E.
AU - Ward, Jerrold M.
N1 - Funding Information:
This work was supported, in part, by USPHS Contract NO1 CO 74102 to Program Resources Inc. and by USPHS Research Grant ROl Al 2271 1 to W.G. We thank Tim O’Leary (AFIP, Washington, DC) for kindly providing the autopsy specimens; Cindy Harris, Kunio Nagashima, and Dianne Krell (PRI, NCI-FCRF, Frederick)forexcellent technical assistance; and Bill Earnshaw, Scott Kaufmann, and Joel Shaper (JHMI, Baltimore) for helpful discussions concerning immu-noaffinlty selection.
PY - 1990/4
Y1 - 1990/4
N2 - A rabbit antiserum prepared against disrupted sucrose-banded HIV-1 virus (strain FRE-3) reacted with antigens present in nuclear inclusions, pathognomonic for human cytomegalovirus (HCMV). This cross-reactivity was observed in autopsy specimens from individuals infected with CMV, in the presence or absence of co-infection with HIV-1. A Towbin immunoassay showed that the serum reacted specifically with the HCMV major capsid protein (MCP, 153 kDa), both in the nuclear fraction of infected cells and in virions. Direct evidence that these proteins share antigenic determinants was provided by the two-way cross-reactivity of affinity-selected antibodies (i.e., anti-MCP with HIV-1 gag precursor Pr55; anti-Pr55 with MCP). All four strains of HCMV tested showed this reactivity, but the counterpart proteins of simian CMV and herpes simplex virus type 1 did not, indicating that the determinant is not common to all herpes group viruses.
AB - A rabbit antiserum prepared against disrupted sucrose-banded HIV-1 virus (strain FRE-3) reacted with antigens present in nuclear inclusions, pathognomonic for human cytomegalovirus (HCMV). This cross-reactivity was observed in autopsy specimens from individuals infected with CMV, in the presence or absence of co-infection with HIV-1. A Towbin immunoassay showed that the serum reacted specifically with the HCMV major capsid protein (MCP, 153 kDa), both in the nuclear fraction of infected cells and in virions. Direct evidence that these proteins share antigenic determinants was provided by the two-way cross-reactivity of affinity-selected antibodies (i.e., anti-MCP with HIV-1 gag precursor Pr55; anti-Pr55 with MCP). All four strains of HCMV tested showed this reactivity, but the counterpart proteins of simian CMV and herpes simplex virus type 1 did not, indicating that the determinant is not common to all herpes group viruses.
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U2 - 10.1016/0042-6822(90)90448-Z
DO - 10.1016/0042-6822(90)90448-Z
M3 - Article
C2 - 1691565
AN - SCOPUS:0025344672
SN - 0042-6822
VL - 175
SP - 595
EP - 599
JO - Virology
JF - Virology
IS - 2
ER -