Literature DB >> 8139029

Assembly of herpes simplex virus (HSV) intermediate capsids in insect cells infected with recombinant baculoviruses expressing HSV capsid proteins.

D R Thomsen1, L L Roof, F L Homa.   

Abstract

The capsid of herpes simplex virus type 1 (HSV-1) is composed of seven proteins, VP5, VP19C, VP21, VP22a, VP23, VP24, and VP26, which are the products of six HSV-1 genes. Recombinant baculoviruses were used to express the six capsid genes (UL18, UL19, UL26, UL26.5, UL35, and UL38) in insect cells. All constructs expressed the appropriate-size HSV proteins, and insect cells infected with a mixture of the six recombinant baculoviruses contained large numbers of HSV-like capsids. Capsids were purified by sucrose gradient centrifugation, and electron microscopy showed that the capsids made in Sf9 cells had the same size and appearance as authentic HSV B capsids. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis demonstrated that the protein composition of these capsids was nearly identical to that of B capsids isolated from HSV-infected Vero cells. Electron microscopy of thin sections clearly demonstrated that the capsids made in insect cells contained the inner electron-translucent core associated with HSV B capsids. In infections in which single capsid genes were left out, it was found that the UL18 (VP23), UL19 (VP5), UL38 (VP19C), and either the UL26 (VP21 and VP24) or the UL26.5 (VP22a) genes were required for assembly of 100-nm capsids. VP22a was shown to form the inner core of the B capsid, since in infections in which the UL26.5 gene was omitted the 100-nm capsids that formed lacked the inner core. The UL35 (VP26) gene was not required for assembly of 100-nm capsids, although assembly of B capsids was more efficient when it was present. These and other observations indicate that (i) the products of the UL18, UL19, UL35, and UL38 genes self-assemble into structures that form the outer surface (icosahedral shell) of the capsid, (ii) the products of the UL26 and/or UL26.5 genes are required (as scaffolds) for assembly of 100-nm capsids, and (iii) the interaction of the outer surface of the capsid with the scaffolding proteins requires the product of the UL18 gene (VP23).

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Year:  1994        PMID: 8139029      PMCID: PMC236722     

Source DB:  PubMed          Journal:  J Virol        ISSN: 0022-538X            Impact factor:   5.103


  45 in total

1.  Characterization of three species of nucleocapsids of equine herpesvirus type-1 (EHV-1).

Authors:  M L Perdue; J C Cohen; M C Kemp; C C Randall; D J O'Callaghan
Journal:  Virology       Date:  1975-03       Impact factor: 3.616

2.  Identification of disulfide-linked protein complexes in the nucleocapsids of herpes simplex virus type 2.

Authors:  M Zweig; C J Heilman; B Hampar
Journal:  Virology       Date:  1979-04-30       Impact factor: 3.616

3.  Electron microscopic studies of temperature-sensitive mutants of herpes simplex virus type 1.

Authors:  P A Schaffer; J P Brunschwig; R M McCombs; M Benyesh-Melnick
Journal:  Virology       Date:  1974-12       Impact factor: 3.616

4.  Proteins specified by herpes simplex virus. V. Purification and structural proteins of the herpesvirion.

Authors:  P G Spear; B Roizman
Journal:  J Virol       Date:  1972-01       Impact factor: 5.103

5.  Studies of the molecular anatomy of the L-M cell strain of equine herpes virus type 1: proteins of the nucleocapsid and intact virion.

Authors:  M L Perdue; M C Kemp; C C Randall; D J O'Callaghan
Journal:  Virology       Date:  1974-05       Impact factor: 3.616

6.  Comparison of the virion proteins specified by herpes simplex virus types 1 and 2.

Authors:  E N Cassai; M Sarmiento; P G Spear
Journal:  J Virol       Date:  1975-11       Impact factor: 5.103

7.  Herpes simplex virus type 1 capsid protein, VP21, originates within the UL26 open reading frame.

Authors:  S Person; S Laquerre; P Desai; J Hempel
Journal:  J Gen Virol       Date:  1993-10       Impact factor: 3.891

8.  Structural analysis of the capsid polypeptides of herpes simplex virus types 1 and 2.

Authors:  G H Cohen; M Ponce de Leon; H Diggelmann; W C Lawrence; S K Vernon; R J Eisenberg
Journal:  J Virol       Date:  1980-05       Impact factor: 5.103

9.  Antigenic variants of herpes simplex virus selected with glycoprotein-specific monoclonal antibodies.

Authors:  T C Holland; S D Marlin; M Levine; J Glorioso
Journal:  J Virol       Date:  1983-02       Impact factor: 5.103

10.  Cloning of herpes simplex virus type 1 sequences representing the whole genome.

Authors:  A L Goldin; R M Sandri-Goldin; M Levine; J C Glorioso
Journal:  J Virol       Date:  1981-04       Impact factor: 5.103

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  98 in total

1.  Packaging-competent capsids of a herpes simplex virus temperature-sensitive mutant have properties similar to those of in vitro-assembled procapsids.

Authors:  F J Rixon; D McNab
Journal:  J Virol       Date:  1999-07       Impact factor: 5.103

2.  Roles of triplex and scaffolding proteins in herpes simplex virus type 1 capsid formation suggested by structures of recombinant particles.

Authors:  A Saad; Z H Zhou; J Jakana; W Chiu; F J Rixon
Journal:  J Virol       Date:  1999-08       Impact factor: 5.103

3.  ATP-Dependent localization of the herpes simplex virus capsid protein VP26 to sites of procapsid maturation.

Authors:  J H Chi; D W Wilson
Journal:  J Virol       Date:  2000-02       Impact factor: 5.103

4.  Lytic replication of Kaposi's sarcoma-associated herpesvirus results in the formation of multiple capsid species: isolation and molecular characterization of A, B, and C capsids from a gammaherpesvirus.

Authors:  K Nealon; W W Newcomb; T R Pray; C S Craik; J C Brown; D H Kedes
Journal:  J Virol       Date:  2001-03       Impact factor: 5.103

5.  Capsid structure of Kaposi's sarcoma-associated herpesvirus, a gammaherpesvirus, compared to those of an alphaherpesvirus, herpes simplex virus type 1, and a betaherpesvirus, cytomegalovirus.

Authors:  B L Trus; J B Heymann; K Nealon; N Cheng; W W Newcomb; J C Brown; D H Kedes; A C Steven
Journal:  J Virol       Date:  2001-03       Impact factor: 5.103

6.  Mechanism of scaffolding-directed virus assembly suggested by comparison of scaffolding-containing and scaffolding-lacking P22 procapsids.

Authors:  P A Thuman-Commike; B Greene; J A Malinski; M Burbea; A McGough; W Chiu; P E Prevelige
Journal:  Biophys J       Date:  1999-06       Impact factor: 4.033

7.  Residues of VP26 of herpes simplex virus type 1 that are required for its interaction with capsids.

Authors:  Prashant Desai; Jean-Claude Akpa; Stanley Person
Journal:  J Virol       Date:  2003-01       Impact factor: 5.103

8.  Cytomegalovirus capsid protease: biological substrates are cleaved more efficiently by full-length enzyme (pUL80a) than by the catalytic domain (assemblin).

Authors:  Steve M Fernandes; Edward J Brignole; Kanchan Taori; Wade Gibson
Journal:  J Virol       Date:  2011-01-26       Impact factor: 5.103

9.  Release of the catalytic domain N(o) from the herpes simplex virus type 1 protease is required for viral growth.

Authors:  L Matusick-Kumar; P J McCann; B J Robertson; W W Newcomb; J C Brown; M Gao
Journal:  J Virol       Date:  1995-11       Impact factor: 5.103

10.  The bovine herpesvirus 1 maturational proteinase and scaffold proteins can substitute for the homologous herpes simplex virus type 1 proteins in the formation of hybrid type B capsids.

Authors:  E J Haanes; D R Thomsen; S Martin; F L Homa; D E Lowery
Journal:  J Virol       Date:  1995-11       Impact factor: 5.103

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