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Peripheral blood lymphocytes from healthy, HIV sero-negative blood donors have been in vitro immunized using penv9, a recombinant fragment of the envelope of HIV-1. This primary in vitro immunization followed by Epstein-Barr virus (EBV) transformation and somatic cell fusion subsequently gave rise to several specific anti-penv9 monoclonal antibodies (MO28, MO30 and MO43) of μ isotype. The hybridomas have been kept in culture for over 6 months and the antibody productivity for MO30 was measured to 18 μg × (24 hr × 106 cells)-1. The fine specificity of the antibodies was mapped by a peptide inhibition enzyme immunoassay, using overlapping synthetic pentadeca peptides covering the whole penv9. These human monoclonal antibodies exhibited a similar epitope specificity directed against a non-sequential determinant, including the amino acids 632–646, 677–681 and 687–691. This specificity is very rarely found in immune sera from sero-positive patients and presently not reported in human monoclonal antibodies derived from in vivo immunized individuals, indicating that different antibody specificities can be obtained by the in vitro immunization technology. These human monoclonal antibodies did not neutralize HIV. The results presented here demonstrate the feasability of generating human monoclonal antibodies against HIV by primary in vitro immunizations, thereby avoiding the use of lymphocytes derived from infected patients when human monoclonal antibodies for therapeutic purposes are to be produced. [ABSTRACT FROM AUTHOR]

Human-mouse hybridoma cell lines producing human monoclonal antibodies against the cardiac glycoside digoxin were established after in vitro immunization or direct immortalization of human peripheral blood lymphocytes with digoxin. Three antibodies, designated MO6, LH92 and LH114, displayed different patterns of fine specificity against digoxin and several digoxin analogues, as elucidated by inhibition ELISA. All three monoclonal antibodies had μ heavy chains, two of them (MO6 and LH114) had κ light chains and one (LH92) λ light chains. DNA encoding the variable regions of both heavy and light chains of the three antibodies were amplified from cDNA using the polymerase chain reaction (PCR). The nucleotide sequences of the amplified DNA were determined after subcloning of PCR fragments in MI3 vectors. The deduced amino acid sequences revealed considerable sequence differences in the complementarity determining regions between the three antibodies. [ABSTRACT FROM AUTHOR]

The article presents information on author index of the December 1, 1986, issue of the periodical "Immunology." Some of the articles as their authors are, "The Ig Class Distribution of Anti-Phosphoryl Choline Responses in Mice Infected With Parasitic Nematodes," by N.M. Almond and R.M.F. Parkhouse, "Passively Acquired Antibodies to Respiratory Syncytial Virus Impair the Secondary Cytotoxic T-cell Response in the Neonatal Mouse," by C.R.M. Bangham, "Production and Characterization of Pepsin Fragments of Human IgA I to Determine Domain-Specificity of Monoclonal Anti-4gA Antibodies," by J. Biewenga, A. Faber, J.C. Pronk, J.J. Haauman, and others.