Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.7.49 (reverse transcriptase)
 31,746 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

B lymphocytes committed to the production of antibodies binding to antigens on pathogenic bacteria and viruses (natural antibodies) are common components of the normal human B cell repertoire. A major proportion of natural antibodies is capable of binding multiple antigens (polyreactive antibodies). Using B cells from three HIV-1 seronegative healthy subjects, and purified HIV-1 and beta-galactosidase from Escherichia coli as selecting antigen, we generated three natural IgM mAb to HIV-1 and a natural IgM mAb to beta-galactosidase. The three HIV-1-selected antibodies (mAb102, mAb103, and mAb104) were polyreactive. They bound with different affinities (Kd = 10(-6) to 10(-8) M) to the HIV-1 envelope gp160, the p24 core protein, and the p66 reverse transcriptase, but not to the 120 glycosylated env protein. They also bound to beta-galactosidase (Kd approximately 10(-7) M), tetanus toxoid, and various various self antigens. In contrast, the natural mAb selected for binding to beta-galactosidase (mAb207.F1) was monoreactive, in that it bound with a high affinity (Kd < 10(-8) M) to this antigen, but to none of the other antigens tested, including HIV-1. Structural analysis of the VH and VL segments revealed that the natural mAb utilized three segments of the VHIV gene family and one of the VHIII family, in conjunction with VL segments of the V lambda I, V lambda II, V lambda III, or V kappa IV subgroups. In addition, the natural mAb VH and VL segments were in unmutated or virtually unmutated (germline) configuration, including those of the monoreactive mAb207.F1 to beta-galactosidase, and were identical or closely related to those utilized by specific autoantibodies or specific antibodies to viral and/or bacterial pathogens. Thus, the present data show that both polyreactive and monoreactive natural antibodies to foreign antigen can be isolated from the normal human B cell repertoire. They also suggest that the VH and VL segments of not only polyreactive but also monoreactive natural antibodies can be encoded in unmutated or minimally mutated genes, and possibly provide the templates for the specific high affinity antibodies elicited by self or foreign antigens.
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PMID:Structure of the VH and VL segments of polyreactive and monoreactive human natural antibodies to HIV-1 and Escherichia coli beta-galactosidase. 831 22

Production of defective virus particles during the early stage of Rous sarcoma virus (RSV) infection of chicken embryo fibroblasts (CEF) was examined. RSV harvested 2 days post infection (2pi) had 10 to 30 times lower specific infectivity (focus forming units/unit reverse transcriptase activity) than 5pi harvest. Virus particles produced on day 2 contained less env proteins than particles harvested on day 5. The amount of other viral proteins was equal in particles harvested on day 2 and day 5. Analysis of infected cells revealed that these cells synthesized less env proteins on day 2 than on day 5. RSV RNA in infected cells was spliced normally on day 2. Infection at a low multiplicity of infection (moi) prolonged the production of defective particles. When infection was initiated by a low moi (0.01), particles harvested on day 5 had the same characteristics as 2pi particles after infection with a high moi (1.0). We conclude that the low infectivity of early harvest is due to the reduced amount of env proteins in virus particles, which is a consequence of the reduced env protein synthesis.
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PMID:Production of env-deficient rous sarcoma virus (RSV) early after infection. 915 53


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