Directed Selection of Recombinant Human Monoclonal Antibodies to Herpes Simplex Virus Glycoproteins from Phage Display Libraries on JSTOR

Directed Selection of Recombinant Human Monoclonal Antibodies to Herpes Simplex Virus Glycoproteins from Phage Display Libraries on JSTOR

Directed Selection of Recombinant Human Monoclonal Antibodies to Herpes Simplex Virus Glycoproteins from Phage Display Libraries on JSTOR
A total of 122 clinical isolates of herpes simplex virus (HSV) from 107 patients were typed by using an indirect immunoperoxidase technique with commercially available type-specific rabbit antisera, recently developed mouse monoclonal antibodies to HSV types 1 and 2, and restriction endonuclease analysis of viral DNA. After removal of antibody reactivity to constant region determinants by absorption with polyclonal mouse immunoglobulins and a monoclonal antibody of the same subclass as the anti-gD monoclonal, the anti-idiotypic (anti-id) antibody reacted specifically with anti-gD. The development of Hybridoma Technology by Kohler and Milstein[1,2] has provided the means to partition the complex antibody responses into their individual components. Functional depletion of CD4+ cells was documented by the loss of delayed-type hypersensitivity responsiveness, while CD8+ cell depletion was accompanied by abrogation of cytotoxic lymphocyte activity. In a low dose challenge model, neutralizing activity of antibody alone was associated with protection in vivo (P less than 0.001). Our data show that the neutralization capacity of MAb 2c is dependent on cross-linkage of gB trimers. The immunophenotype of the neoplastic cells was B CD19+ CD20+ CD22+ with coexpression of CD10 and CD23 and with clonal kappa light chain rearrangement.

For example, if the current year is 2008 and a journal has a 5 year moving wall, articles from the year 2002 are available. These observations imply that either pentons are composed of some other protein(s) or that they also contain VP5, but in a conformation sufficiently different from that assumed in hexons as to transform its antigenic character. Full text Full text is available as a scanned copy of the original print version. Complete: Journals that are no longer published or that have been combined with another title.

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