Twenty‐seven soft tissue tumors composed of benign adipose tissue are presented featuring extensive local invasion and recurrence. Infiltrating angiolipomas and infiltrating lipomas are two distinct entities with different clinical and histologic features. The surgical approach demands wide local excision assisted by frozen section analysis to assure adequacy of removal. Extensive histologic sampling is mandatory to demonstrate the infiltrative character of the tumor and yet eliminate from consideration liposarcoma with which it may be confused. Although locally recurrent, neither has yet undergone malignant transformation.

SUMMARYA 7000 Mr cleavage fragment of the F 1 subunit that carries the major neutralization epitope has been identified by chemical and enzymatic cleavage of the fusion protein of respiratory syncytial (RS) virus (Long strain) with an efficient RS virus-neutralizing monoclonal antibody. Based on the published mRNA-deduced sequence of the A2 strain, coupled to the hydropathicity profile and prediction of protein conformation, the neutralization epitope has tentatively been localized on the first third of the F1 protein N-terminal, probably in the region of amino acids 215Ser to 236Glu. Analysis of three peptides covering different portions of the 212Cys to 236Glu region of the F 1 fusion protein identified a peptide (Cys. 216Ash to 236Glu) that reacted strongly with the neutralizing monoclonal antibody and that was efficient in blocking neutralization and in plaque-reducing assays, confirming that the neutralization epitope was localized in that region. Further analysis with two other synthetic peptides (212Cys to 222Glu and Cys.221Ile to 236Glu) indicated that the dodecapeptide Ile-Glu-Phe-Gln-LysAsn-Asn-Arg-Leu-Leu-Glu mimicked either the whole or a major part of the neutralization epitope. This opens a promising avenue for the simple design of a synthetic peptide vaccine to control RS virus infection. INTRODUCTIONThe genus Pneumovirus of the Paramyxoviridae family consists of human and bovine strains of respiratory syncytial (RS) virus and pneumonia virus of mice. Human RS virus, an important pathogen in young children (Belshe et al., 1984), is thought to be a monotypic strain though minor differences in cross-neutralization assays have been noted. Using monoclonal antibodies (MAbs), Mufson et al. (1985) have been able to separate different isolates into subgroups A and B; however, studies by Prince et al. (1985) suggest that antigenic differences detected in vitro disappear when virus strains are compared in vivo. Recently, using a neutralizing MAb produced against the Long strain of RS virus, a major and highly conserved neutralization epitope was identified which was present on human, bovine and caprine strains of RS virus but not on pneumonia virus of mice. This epitope is localized on the F 1 fragment of the fusion glycoprotein (Trudel et al., 1986(Trudel et al., , 1987.The fusion glycoprotein is found as a 125K Mr dimer on the viral envelope and is involved in cell fusion leading to the formation of syncytia and cell penetration. It is composed of two disulphide-linked subunits: F1 with a reported Mr varying from 43K to 50K and F2 from 19K to 25K (Walsh et al., 1985, 1986;Trudel et al., 1986).Expression by recombinant vaccinia viruses of the major and fusion glycoproteins of RS virus (Olmsted et al., 1986) confirmed previous work carried out with MAbs and purified solubilized proteins showing the predominant role of the fusion glycoprotein in inducing immunity

We selected in vitro human immunodeficiency virus type 1 variants that are resistant to each of 2',3'-dideoxycytidine (ddC) and the racemic mixture of 2',3'-dideoxy-3'-thiacytidine (BCH-189). The median effective concentrations of ddC and BCH-189 obtained for the resistant viruses ranged between 10 and 50 times above those for parental wild-type strains, and extensive cross-resistance was observed against 2',3'-dideoxyinosine (ddI) but not 3'-azido-3'-deoxythymidine (AZT). Two dimer compounds, in which either AZT and ddI or AZT and BCH-189 were linked through phosphodiester linkages, did not permit the emergence of variants resistant to BCH-189, ddI, or AZT but were ineffective at inhibiting the replication of AZT-resistant viruses.

A surface probability method was used to select a decapeptide homologous to residues 993 to 1002 of the peplomer protein E2 of murine hepatitis virus strain JHM, a neurotropic coronavirus. This sequence of amino acids corresponded to a minor peak on a hydrophilicity plot. Immunization of mice with the chemically synthesized peptide coupled to keyhole limpet hemocyanin elicited high levels of neutralizing antibody and protected against lethal virus challenge. Protection correlated with a critical level of antipeptide antibody, which could be reached after a single inoculation. These results suggest that an appropriate antibody response to a highly restricted, surface-exposed domain of this viral protein is critical in determining the outcome of infection of the central nervous system. This sequence is located in the C-terminal fifth of the E2 peplomers, between two predicted coiled-coil structures.