Glycoproteins of herpes simplex virus type 2 as defined by monoclonal antibodies

Balachandran, N.; Harnish, Delsworth G.; Rawls, William E.; Bacchetti, Silvia

doi:10.1128/jvi.44.1.344-355.1982

Cited by 89 publications

(57 citation statements)

References 24 publications

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“…Previous studies demonstrated that monoclonal antibodies directed against herpes simplex virus types 1 and 2 (2,3,32,34,54), human cytomegalovirus (33), Epstein-Barr virus (46), varicella-zoster virus (15,27), and pseudorabiesvirus (18) can precipitate several polypeptides with different electrophoretic mobilities. Because a similar phenomenon occurred with BHV-1, several approaches were used to analyze the relationships among those BHV-1 glycoproteins that appeared to be complexed.…”

Section: Discussionmentioning

confidence: 99%

Synthesis and processing of bovine herpesvirus 1 glycoproteins

Hurk¹,

Babiuk²

1986

J Virol

107

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Four unique glycoproteins or glycoprotein complexes were recognized by a panel of monoclonal antibodies to bovine herpesvirus 1 (BHV-1), i.e., GVP 6/lla/16 (130,000-molecular-weight glycoprotein [130K glycoprotein]/74K/55K), GVP 7 (108K), GVP 3/9 (180K/91K), and GVP llb (71K). The absence of any antigenic or structural relationship between GVP lla and GVP llb, which were previously identified as one glycoprotein, GVP 11, demonstrated that these two GVP 11 species are unique glycoproteins. GVP 3 and GVP 9 showed complete sequence homology, as shown by the identity of their antigenic determinants and by partial peptide mapping. This observation, as well as the ratio of their apparent molecular weights, indicated that GVP 3 (180K) is a dimeric form of GVP 9 (91K). GVP 6 and GVP lla, as well as GVP 6 and GVP 16, showed at least partial sequence homology, since they shared several antigenic determinants and peptides. In addition, GVP 6, GVP lla, and GVP 16 were derived from one primary precursor. These results, as well as the ratio of their apparent molecular weights, indicated that the GVP 6/lla/16 complex consists of two forms: one in which GVP 6 (130K) is uncleaved and the other one in which GVP 6 is cleaved and composed of GVP 11a (74K) and GVP 16 (55K), linked by disulfide bridges. An antigenically distinct precursor to each of the four BHV-1 glycoproteins or glycoprotein complexes was identified by monoclonal antibodies. These precursors, pGVP 6 (117K), pGVP Ila (62K), pGVP 7 (lOOK), pGVP 9 (69K), and pGVP llb (63K) were sensitive to endo-o-N-acetylglucosaminidase H treatment, indicating that they represent the partially glycosylated highmannose-type intermediate forms generated by cotranslational glycosylation of the primary, unglycosylated precursors to GVP 6/lla/16, GVP 7, GVP 3/9, and GVP llb, which were identified as having apparent molecular weights of 105,000, 90,000, 61,000, and 58,000, respectively. A new nomenclature for the BHV-1 glycoproteins, based on roman numerals, is proposed. 401 on July 6, 2020 by guest http://jvi.asm.org/ Downloaded from bated with a 1:1,000 dilution of ascites fluid and then with a 1:1,000 dilution of rabbit anti-mouse IgG (Cooper Biomedical, Inc., West Chester, Pa.) and 5 x 105 to 1 x 106 cpm of 125I-labeled protein A (Pharmacia). Finally, the nitrocellulose strips were dried and analyzed by autoradiography on 3M X-ray film.

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Section: Discussionmentioning

confidence: 99%

Synthesis and processing of bovine herpesvirus 1 glycoproteins

Hurk¹,

Babiuk²

1986

J Virol

107

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“…Thus these reports have, for the most part, had to use at least two or more antibodies for both HSV-1 and HSV-2. The added complication of the host cell's glycosylation machinery has led us to seek other markers besides those for the major glycoproteins [Pereira et al, 1981[Pereira et al, , 1982Goldstein et al, 1983;Balachandran et al, 1982a;Peterson et al, 1983;Nilheden et al, 19831. While still not characterized, the late emergence of the antigens after infection, their occurrence on the unenveloped purified nucleocapsid, and the predominant speckled nuclear immunofluorescent patterns argue strongly against either antibody's being one of the major glycoproteins even though the tentative molecular weight is consistent with gC (HSV-1) or gA/B [Balachandran et al, 1982al. Which late HSV protein has such specificity is an open question.…”

Section: Discussionmentioning

confidence: 99%

“…With the development of the hybridoma techniques of Kohler and Milstein [ 19751 monoclonal antibodies have been prepared which appear to selectively react with HSV-1, HSV-2, or both HSV-1 and HSV-2 [Zweig et al, 1979;Pereira et al, 1980;Killington et al, 1981;Goldstein et al, 1983;Howes et al, 1979;Balachandran et al, 1979. These antibodies have been used to extract labeled virus proteins from infected cells and for fluorescent antibody visualization of the HSV-associated proteins in infected cells [Balachandran et al, 1982al.…”

Section: Introductionmentioning

confidence: 99%

Identification and typing of herpes simplex virus types 1 and 2 by monoclonal antibodies, sensitivity to the drug (E)‐5‐(2‐bromovinyl)‐2′‐deoxyuridine, and restriction endonuclease analysis of viral DNA

Zimmerman

Mundon

Croson

et al. 1985

Journal of Medical Virology

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With development of antiviral drugs, the need to identify a virus as to drug sensitivity becomes increasingly of importance. The compound (E)-5-(2-bromovinyl)-2'-deoxyuridine (BVDU) has been shown to be much more inhibitory to the replication of herpes simplex virus type 1 (HSV-1) and varicella-zoster virus as opposed to herpes simplex virus type 2 (HSV-2). We have typed over 170 isolates, using an immunofluorescent technique and sensitivity to the drug BVDU. These results were then compared to the typing of isolates by analysis of viral DNA after restriction endonuclease digestion (EcoRI). Without exception the results were in agreement between the monoclonal antibody results and sensitivity to the drug BVDU. Furthermore, the typing with monoclonal antibodies was also in excellent agreement with the DNA analysis. Only those isolates inhibited with BVDU showed DNA characteristics of HSV-1 and reacted only with the S-200 antibody. On the other hand, those isolates which reacted with the monoclonal antibody S-141 were insensitive to BVDU, and again this was in agreement with the DNA analysis. These results could provide the basis for developing a diagnostic test using the two monoclonal antibodies to type either isolates or direct smears and to use the results as a basis for possible drug therapy.

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“…In another study with intertypic recombinant viruses (20), an HSV-2 glycoprotein of 63,000 daltons with no apparent HSV-1 counterpart was mapped between 0.55 and 0.65 m.u. Monoclonal antibodies (MABs) to HSV-2 glycoproteins also detected a small glycoprotein with a molecular weight of 60,000 which could be chased into higher-molecular-weight forms of 66,000 and 79,000 (3,4) and was designated gF. Results from two studies with monoclonal antibodies (44,45) showed that HSV-2 gF shared antigenic determinants with HSV-1 gC.…”

mentioning

confidence: 99%

Characterization of the gene encoding herpes simplex virus type 2 glycoprotein C and comparison with the type 1 counterpart

Swain¹,

Peet²,

Galloway³

1985

J Virol

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The gene encoding the glycoprotein C (gC) of herpes simplex virus type 1 maps to the region of the viral genome from 0.62 to 0.64. Recently, a herpes simplex virus type 2 glycoprotein previously designated gF and now designated gC was mapped to a homologous location. Analysis of the herpes simplex virus type 2 mRNA species encoded in this region revealed a major transcript of 2.5 kilobases, a 0.73-kilobase transcript (the 5' ends of which were mapped by primer extension), and several minor species, all nearly identical to the herpes simplex virus type 1 pattern. A polypeptide of ca. 60,000 daltons was identified by in vitro translation of hybrid-selected mRNA. A smaller protein of ca. 20,000 daltons was also mapped to this region. The nucleotide sequence of a 3.4-kilobase segment of DNA encompassing gC was determined, and an open reading frame of 1,440 nucleotides specifying a 480-amino acid protein with properties consistent with that of a glycoprotein was identified. Comparative DNA sequence analysis showed regions of limited homology within the coding sequences for gC and a deletion which results in 31 fewer amino acids in the gC-2 near the amino terminus of the protein. The carboxy termini of gC-1 and gC-2 are very similar, as are the 20,000-dalton proteins. 561 on July 6, 2020 by guest

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Glycoproteins of herpes simplex virus type 2 as defined by monoclonal antibodies

Cited by 89 publications

References 24 publications

Synthesis and processing of bovine herpesvirus 1 glycoproteins

Synthesis and processing of bovine herpesvirus 1 glycoproteins

Identification and typing of herpes simplex virus types 1 and 2 by monoclonal antibodies, sensitivity to the drug (E)‐5‐(2‐bromovinyl)‐2′‐deoxyuridine, and restriction endonuclease analysis of viral DNA

Characterization of the gene encoding herpes simplex virus type 2 glycoprotein C and comparison with the type 1 counterpart

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