EFFICIENT NEUTRALIZATION OF PRIMARY ISOLATES OF HIV-1 BY A RECOMBINANT HUMAN MONOCLONAL-ANTIBODY

被引:963
作者
BURTON, DR
PYATI, J
KODURI, R
SHARP, SJ
THORNTON, GB
PARREN, PWHI
SAWYER, LSW
HENDRY, RM
DUNLOP, N
NARA, PL
LAMACCHIA, M
GARRATTY, E
STIEHM, ER
BRYSON, YJ
CAO, YZ
MOORE, JP
HO, DD
BARBAS, CF
机构
[1] SCRIPPS RES INST, DEPT BIOL MOLEC, LA JOLLA, CA 92037 USA
[2] RW JOHNSON PHARMACEUT RES INST, SAN DIEGO, CA 92121 USA
[3] CALIF DEPT HLTH SERV, VIRAL & RICKETTSIAL DIS LAB, BERKELEY, CA 94704 USA
[4] NCI, FREDERICK CANC RES & DEV CTR, TUMOR CELL BIOL LAB, VIRUS BIOL SECT, FREDERICK, MD 21702 USA
[5] UNIV CALIF LOS ANGELES, SCH MED, DEPT PEDIAT, LOS ANGELES, CA 90024 USA
[6] NYU, SCH MED, AARON DIAMOND AIDS RES CTR, NEW YORK, NY 10016 USA
关键词
D O I
10.1126/science.7973652
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The ability of antibodies to neutralize diverse primary isolates of human immunodeficiency virus-type 1 in vitro has been questioned, with implications for the likely efficacy of vaccines. A recombinant human antibody to envelope glycoprotein gp120 was generated and used to show that primary isolates are not refractory to antibody neutralization. The recombinant antibody neutralized more than 75 percent of the primary isolates tested at concentrations that could be achieved by passive immunization, for example, to interrupt maternal-fetal transmission of virus. The broad specificity and efficacy of the antibody implies the conservation of a structural feature on gp120, which could be important in vaccine design.
引用
收藏
页码:1024 / 1027
页数:4
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