Abstract
We have used the yeast GAL4 two-hybrid system to examine interactions between the human cytomegalovirus (HCMV) major capsid protein (MCP, encoded by UL86) and the precursor assembly protein (pAP, encoded by UL80.5 and cleaved at its carboxyl end to yield AP) and found that (i) the pAP interacts with the MCP through residues located within the carboxy-terminal 21 amino acids of the pAP, called the carboxyl conserved domain (CCD); (ii) the pAP interacts with itself through a separate region, called the amino conserved domain (ACD), located between amino acids His34 and Arg52 near the amino end of the molecule; (iii) the simian CMV (SCMV) pAP and AP can interact with or replace their HCMV counterparts in these interactions, whereas the herpes simplex virus pAP and AP homologs cannot; and (iv) the HCMV and SCMV maturational proteinase precursors (ACpra, encoded by UL80a and APNG1, respectively) can interact with the pAP and MCP. The ACD and CCD amino acid sequences are highly conserved among members of the betaherpesvirus group and appear to have counterparts in the alpha- and gammaherpesvirus pAP homologs. Deleting the ACD from the HCMV pAP, or substituting Ala for a conserved Leu in the ACD, eliminated detectable pAP self-interaction and also substantially reduced MCP binding in the two-hybrid assay. This finding indicates that the pAP self-interaction influences the pAP-MCP interaction. Immunofluorescence studies corroborated the pAP-MCP interaction detected in the GAL4 two-hybrid experiments and showed that nuclear transport of the MCP was mediated by pAP but not AP. We conclude that the pAP interacts with the MCP, that this interaction is mediated by the CCD and is influenced by pAP self-interaction, and that one function of the pAP-MCP interaction may be to provide a controlled mechanism for transporting the MCP into the nucleus.
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- Adams G. A., Rose J. K. Structural requirements of a membrane-spanning domain for protein anchoring and cell surface transport. Cell. 1985 Jul;41(3):1007–1015. doi: 10.1016/s0092-8674(85)80081-7. [DOI] [PubMed] [Google Scholar]
- Albrecht J. C., Nicholas J., Biller D., Cameron K. R., Biesinger B., Newman C., Wittmann S., Craxton M. A., Coleman H., Fleckenstein B. Primary structure of the herpesvirus saimiri genome. J Virol. 1992 Aug;66(8):5047–5058. doi: 10.1128/jvi.66.8.5047-5058.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Baer R., Bankier A. T., Biggin M. D., Deininger P. L., Farrell P. J., Gibson T. J., Hatfull G., Hudson G. S., Satchwell S. C., Séguin C. DNA sequence and expression of the B95-8 Epstein-Barr virus genome. Nature. 1984 Jul 19;310(5974):207–211. doi: 10.1038/310207a0. [DOI] [PubMed] [Google Scholar]
- Baker T. S., Newcomb W. W., Booy F. P., Brown J. C., Steven A. C. Three-dimensional structures of maturable and abortive capsids of equine herpesvirus 1 from cryoelectron microscopy. J Virol. 1990 Feb;64(2):563–573. doi: 10.1128/jvi.64.2.563-573.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Baldick C. J., Jr, Shenk T. Proteins associated with purified human cytomegalovirus particles. J Virol. 1996 Sep;70(9):6097–6105. doi: 10.1128/jvi.70.9.6097-6105.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Beaudet-Miller M., Zhang R., Durkin J., Gibson W., Kwong A. D., Hong Z. Virus-specific interaction between the human cytomegalovirus major capsid protein and the C terminus of the assembly protein precursor. J Virol. 1996 Nov;70(11):8081–8088. doi: 10.1128/jvi.70.11.8081-8088.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Breeden L., Nasmyth K. Regulation of the yeast HO gene. Cold Spring Harb Symp Quant Biol. 1985;50:643–650. doi: 10.1101/sqb.1985.050.01.078. [DOI] [PubMed] [Google Scholar]
- Chee M. S., Bankier A. T., Beck S., Bohni R., Brown C. M., Cerny R., Horsnell T., Hutchison C. A., 3rd, Kouzarides T., Martignetti J. A. Analysis of the protein-coding content of the sequence of human cytomegalovirus strain AD169. Curr Top Microbiol Immunol. 1990;154:125–169. doi: 10.1007/978-3-642-74980-3_6. [DOI] [PubMed] [Google Scholar]
- Chee M., Rudolph S. A., Plachter B., Barrell B., Jahn G. Identification of the major capsid protein gene of human cytomegalovirus. J Virol. 1989 Mar;63(3):1345–1353. doi: 10.1128/jvi.63.3.1345-1353.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chevray P. M., Nathans D. Protein interaction cloning in yeast: identification of mammalian proteins that react with the leucine zipper of Jun. Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):5789–5793. doi: 10.1073/pnas.89.13.5789. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chien C. T., Bartel P. L., Sternglanz R., Fields S. The two-hybrid system: a method to identify and clone genes for proteins that interact with a protein of interest. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9578–9582. doi: 10.1073/pnas.88.21.9578. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cohen G. H., Ponce de Leon M., Diggelmann H., Lawrence W. C., Vernon S. K., Eisenberg R. J. Structural analysis of the capsid polypeptides of herpes simplex virus types 1 and 2. J Virol. 1980 May;34(2):521–531. doi: 10.1128/jvi.34.2.521-531.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Davison A. J., Scott J. E. The complete DNA sequence of varicella-zoster virus. J Gen Virol. 1986 Sep;67(Pt 9):1759–1816. doi: 10.1099/0022-1317-67-9-1759. [DOI] [PubMed] [Google Scholar]
- Davison M. D., Rixon F. J., Davison A. J. Identification of genes encoding two capsid proteins (VP24 and VP26) of herpes simplex virus type 1. J Gen Virol. 1992 Oct;73(Pt 10):2709–2713. doi: 10.1099/0022-1317-73-10-2709. [DOI] [PubMed] [Google Scholar]
- Desai P., Person S. Molecular interactions between the HSV-1 capsid proteins as measured by the yeast two-hybrid system. Virology. 1996 Jun 15;220(2):516–521. doi: 10.1006/viro.1996.0341. [DOI] [PubMed] [Google Scholar]
- Estojak J., Brent R., Golemis E. A. Correlation of two-hybrid affinity data with in vitro measurements. Mol Cell Biol. 1995 Oct;15(10):5820–5829. doi: 10.1128/mcb.15.10.5820. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fields S., Song O. A novel genetic system to detect protein-protein interactions. Nature. 1989 Jul 20;340(6230):245–246. doi: 10.1038/340245a0. [DOI] [PubMed] [Google Scholar]
- Finley R. L., Jr, Brent R. Interaction mating reveals binary and ternary connections between Drosophila cell cycle regulators. Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12980–12984. doi: 10.1073/pnas.91.26.12980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Friedmann A., Coward J. E., Rosenkranz H. S., Morgan C. Electron microscopic studies on assembly of herpes simplex virus upon removal of hydroxyurea block. J Gen Virol. 1975 Feb;26(2):171–181. doi: 10.1099/0022-1317-26-2-171. [DOI] [PubMed] [Google Scholar]
- Gao M., Matusick-Kumar L., Hurlburt W., DiTusa S. F., Newcomb W. W., Brown J. C., McCann P. J., 3rd, Deckman I., Colonno R. J. The protease of herpes simplex virus type 1 is essential for functional capsid formation and viral growth. J Virol. 1994 Jun;68(6):3702–3712. doi: 10.1128/jvi.68.6.3702-3712.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gerace L., Burke B. Functional organization of the nuclear envelope. Annu Rev Cell Biol. 1988;4:335–374. doi: 10.1146/annurev.cb.04.110188.002003. [DOI] [PubMed] [Google Scholar]
- Gibson W., Baxter M. K., Clopper K. S. Cytomegalovirus "missing" capsid protein identified as heat-aggregable product of human cytomegalovirus UL46. J Virol. 1996 Nov;70(11):7454–7461. doi: 10.1128/jvi.70.11.7454-7461.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gibson W., Clopper K. S., Britt W. J., Baxter M. K. Human cytomegalovirus (HCMV) smallest capsid protein identified as product of short open reading frame located between HCMV UL48 and UL49. J Virol. 1996 Aug;70(8):5680–5683. doi: 10.1128/jvi.70.8.5680-5683.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gibson W., Roizman B. Proteins specified by herpes simplex virus. 8. Characterization and composition of multiple capsid forms of subtypes 1 and 2. J Virol. 1972 Nov;10(5):1044–1052. doi: 10.1128/jvi.10.5.1044-1052.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gibson W. Structural and nonstructural proteins of strain Colburn cytomegalovirus. Virology. 1981 Jun;111(2):516–537. doi: 10.1016/0042-6822(81)90354-8. [DOI] [PubMed] [Google Scholar]
- Gilks C. B., Bear S. E., Grimes H. L., Tsichlis P. N. Progression of interleukin-2 (IL-2)-dependent rat T cell lymphoma lines to IL-2-independent growth following activation of a gene (Gfi-1) encoding a novel zinc finger protein. Mol Cell Biol. 1993 Mar;13(3):1759–1768. doi: 10.1128/mcb.13.3.1759. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gompels U. A., Nicholas J., Lawrence G., Jones M., Thomson B. J., Martin M. E., Efstathiou S., Craxton M., Macaulay H. A. The DNA sequence of human herpesvirus-6: structure, coding content, and genome evolution. Virology. 1995 May 10;209(1):29–51. doi: 10.1006/viro.1995.1228. [DOI] [PubMed] [Google Scholar]
- Griffin A. M. The complete sequence of the capsid p40 gene from infectious laryngotracheitis virus. Nucleic Acids Res. 1990 Jun 25;18(12):3664–3664. doi: 10.1093/nar/18.12.3664. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Haanes E. J., Thomsen D. R., Martin S., Homa F. L., Lowery D. E. 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. J Virol. 1995 Nov;69(11):7375–7379. doi: 10.1128/jvi.69.11.7375-7379.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Heilman C. J., Jr, Zweig M., Stephenson J. R., Hampar B. Isolation of a nucleocapsid polypeptide of herpes simplex virus types 1 and 2 possessing immunologically type-specific and cross-reactive determinants. J Virol. 1979 Jan;29(1):34–42. doi: 10.1128/jvi.29.1.34-42.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hong Z., Beaudet-Miller M., Durkin J., Zhang R., Kwong A. D. Identification of a minimal hydrophobic domain in the herpes simplex virus type 1 scaffolding protein which is required for interaction with the major capsid protein. J Virol. 1996 Jan;70(1):533–540. doi: 10.1128/jvi.70.1.533-540.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Irmiere A., Gibson W. Isolation and characterization of a noninfectious virion-like particle released from cells infected with human strains of cytomegalovirus. Virology. 1983 Oct 15;130(1):118–133. doi: 10.1016/0042-6822(83)90122-8. [DOI] [PubMed] [Google Scholar]
- Irmiere A., Gibson W. Isolation of human cytomegalovirus intranuclear capsids, characterization of their protein constituents, and demonstration that the B-capsid assembly protein is also abundant in noninfectious enveloped particles. J Virol. 1985 Oct;56(1):277–283. doi: 10.1128/jvi.56.1.277-283.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kamens J., Brent R. A yeast transcription assay defines distinct rel and dorsal DNA recognition sequences. New Biol. 1991 Oct;3(10):1005–1013. [PubMed] [Google Scholar]
- Kang K. I., Devin J., Cadepond F., Jibard N., Guiochon-Mantel A., Baulieu E. E., Catelli M. G. In vivo functional protein-protein interaction: nuclear targeted hsp90 shifts cytoplasmic steroid receptor mutants into the nucleus. Proc Natl Acad Sci U S A. 1994 Jan 4;91(1):340–344. doi: 10.1073/pnas.91.1.340. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kennard J., Rixon F. J., McDougall I. M., Tatman J. D., Preston V. G. The 25 amino acid residues at the carboxy terminus of the herpes simplex virus type 1 UL26.5 protein are required for the formation of the capsid shell around the scaffold. J Gen Virol. 1995 Jul;76(Pt 7):1611–1621. doi: 10.1099/0022-1317-76-7-1611. [DOI] [PubMed] [Google Scholar]
- King J., Casjens S. Catalytic head assembling protein in virus morphogenesis. Nature. 1974 Sep 13;251(5471):112–119. doi: 10.1038/251112a0. [DOI] [PubMed] [Google Scholar]
- Ladin B. F., Blankenship M. L., Ben-Porat T. Replication of herpesvirus DNA. V. Maturation of concatemeric DNA of pseudorabies virus to genome length is related to capsid formation. J Virol. 1980 Mar;33(3):1151–1164. doi: 10.1128/jvi.33.3.1151-1164.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lee J. Y., Irmiere A., Gibson W. Primate cytomegalovirus assembly: evidence that DNA packaging occurs subsequent to B capsid assembly. Virology. 1988 Nov;167(1):87–96. doi: 10.1016/0042-6822(88)90057-8. [DOI] [PubMed] [Google Scholar]
- Liu F. Y., Roizman B. The herpes simplex virus 1 gene encoding a protease also contains within its coding domain the gene encoding the more abundant substrate. J Virol. 1991 Oct;65(10):5149–5156. doi: 10.1128/jvi.65.10.5149-5156.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Long E. O., Rosen-Bronson S., Karp D. R., Malnati M., Sekaly R. P., Jaraquemada D. Efficient cDNA expression vectors for stable and transient expression of HLA-DR in transfected fibroblast and lymphoid cells. Hum Immunol. 1991 Aug;31(4):229–235. doi: 10.1016/0198-8859(91)90092-n. [DOI] [PubMed] [Google Scholar]
- Loutsch J. M., Galvin N. J., Bryant M. L., Holwerda B. C. Cloning and sequence analysis of murine cytomegalovirus protease and capsid assembly protein genes. Biochem Biophys Res Commun. 1994 Aug 30;203(1):472–478. doi: 10.1006/bbrc.1994.2206. [DOI] [PubMed] [Google Scholar]
- Matusick-Kumar L., Newcomb W. W., Brown J. C., McCann P. J., 3rd, Hurlburt W., Weinheimer S. P., Gao M. The C-terminal 25 amino acids of the protease and its substrate ICP35 of herpes simplex virus type 1 are involved in the formation of sealed capsids. J Virol. 1995 Jul;69(7):4347–4356. doi: 10.1128/jvi.69.7.4347-4356.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McGeoch D. J., Dalrymple M. A., Davison A. J., Dolan A., Frame M. C., McNab D., Perry L. J., Scott J. E., Taylor P. The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. J Gen Virol. 1988 Jul;69(Pt 7):1531–1574. doi: 10.1099/0022-1317-69-7-1531. [DOI] [PubMed] [Google Scholar]
- Newcomb W. W., Brown J. C., Booy F. P., Steven A. C. Nucleocapsid mass and capsomer protein stoichiometry in equine herpesvirus 1: scanning transmission electron microscopic study. J Virol. 1989 Sep;63(9):3777–3783. doi: 10.1128/jvi.63.9.3777-3783.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Newcomb W. W., Brown J. C. Structure of the herpes simplex virus capsid: effects of extraction with guanidine hydrochloride and partial reconstitution of extracted capsids. J Virol. 1991 Feb;65(2):613–620. doi: 10.1128/jvi.65.2.613-620.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Newcomb W. W., Homa F. L., Thomsen D. R., Ye Z., Brown J. C. Cell-free assembly of the herpes simplex virus capsid. J Virol. 1994 Sep;68(9):6059–6063. doi: 10.1128/jvi.68.9.6059-6063.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Newcomb W. W., Trus B. L., Booy F. P., Steven A. C., Wall J. S., Brown J. C. Structure of the herpes simplex virus capsid. Molecular composition of the pentons and the triplexes. J Mol Biol. 1993 Jul 20;232(2):499–511. doi: 10.1006/jmbi.1993.1406. [DOI] [PubMed] [Google Scholar]
- Nicholas J. Determination and analysis of the complete nucleotide sequence of human herpesvirus. J Virol. 1996 Sep;70(9):5975–5989. doi: 10.1128/jvi.70.9.5975-5989.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nicholson P., Addison C., Cross A. M., Kennard J., Preston V. G., Rixon F. J. Localization of the herpes simplex virus type 1 major capsid protein VP5 to the cell nucleus requires the abundant scaffolding protein VP22a. J Gen Virol. 1994 May;75(Pt 5):1091–1099. doi: 10.1099/0022-1317-75-5-1091. [DOI] [PubMed] [Google Scholar]
- O'Callaghan D. J., Hyde J. M., Gentry G. A., Randall C. C. Kinetics of viral deoxyribonucleic acid, protein, and infectious particle production and alterations in host macromolecular syntheses in equine abortion (herpes) virus-infected cells. J Virol. 1968 Aug;2(8):793–804. doi: 10.1128/jvi.2.8.793-804.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- O'Callaghan D. J., Randall C. C. Molecular anatomy of herpesviruses: recent studies. Prog Med Virol. 1976;22:152–210. [PubMed] [Google Scholar]
- Perdue M. L., Cohen J. C., Kemp M. C., Randall C. C., O'Callaghan D. J. Characterization of three species of nucleocapsids of equine herpesvirus type-1 (EHV-1). Virology. 1975 Mar;64(1):187–204. doi: 10.1016/0042-6822(75)90091-4. [DOI] [PubMed] [Google Scholar]
- Person S., Laquerre S., Desai P., Hempel J. Herpes simplex virus type 1 capsid protein, VP21, originates within the UL26 open reading frame. J Gen Virol. 1993 Oct;74(Pt 10):2269–2273. doi: 10.1099/0022-1317-74-10-2269. [DOI] [PubMed] [Google Scholar]
- Preston V. G., Coates J. A., Rixon F. J. Identification and characterization of a herpes simplex virus gene product required for encapsidation of virus DNA. J Virol. 1983 Mar;45(3):1056–1064. doi: 10.1128/jvi.45.3.1056-1064.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rixon F. J., Cross A. M., Addison C., Preston V. G. The products of herpes simplex virus type 1 gene UL26 which are involved in DNA packaging are strongly associated with empty but not with full capsids. J Gen Virol. 1988 Nov;69(Pt 11):2879–2891. doi: 10.1099/0022-1317-69-11-2879. [DOI] [PubMed] [Google Scholar]
- Robertson B. J., McCann P. J., 3rd, Matusick-Kumar L., Newcomb W. W., Brown J. C., Colonno R. J., Gao M. Separate functional domains of the herpes simplex virus type 1 protease: evidence for cleavage inside capsids. J Virol. 1996 Jul;70(7):4317–4328. doi: 10.1128/jvi.70.7.4317-4328.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Robson L., Gibson W. Primate cytomegalovirus assembly protein: genome location and nucleotide sequence. J Virol. 1989 Feb;63(2):669–676. doi: 10.1128/jvi.63.2.669-676.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Roizman B., Carmichael L. E., Deinhardt F., de-The G., Nahmias A. J., Plowright W., Rapp F., Sheldrick P., Takahashi M., Wolf K. Herpesviridae. Definition, provisional nomenclature, and taxonomy. The Herpesvirus Study Group, the International Committee on Taxonomy of Viruses. Intervirology. 1981;16(4):201–217. doi: 10.1159/000149269. [DOI] [PubMed] [Google Scholar]
- Schacterle G. R., Pollack R. L. A simplified method for the quantitative assay of small amounts of protein in biologic material. Anal Biochem. 1973 Feb;51(2):654–655. doi: 10.1016/0003-2697(73)90523-x. [DOI] [PubMed] [Google Scholar]
- Schenk P., Woods A. S., Gibson W. The 45-kilodalton protein of cytomegalovirus (Colburn) B-capsids is an amino-terminal extension form of the assembly protein. J Virol. 1991 Mar;65(3):1525–1529. doi: 10.1128/jvi.65.3.1525-1529.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sherman G., Bachenheimer S. L. Characterization of intranuclear capsids made by ts morphogenic mutants of HSV-1. Virology. 1988 Apr;163(2):471–480. doi: 10.1016/0042-6822(88)90288-7. [DOI] [PubMed] [Google Scholar]
- Steffy K. R., Schoen S., Chen C. M. Nucleotide sequence of the herpes simplex virus type 2 gene encoding the protease and capsid protein ICP35. J Gen Virol. 1995 Apr;76(Pt 4):1069–1072. doi: 10.1099/0022-1317-76-4-1069. [DOI] [PubMed] [Google Scholar]
- Szilágyi J. F., Cunningham C. Identification and characterization of a novel non-infectious herpes simplex virus-related particle. J Gen Virol. 1991 Mar;72(Pt 3):661–668. doi: 10.1099/0022-1317-72-3-661. [DOI] [PubMed] [Google Scholar]
- Talbot P., Almeida J. D. Human cytomegalovirus: purification of enveloped virions and dense bodies. J Gen Virol. 1977 Aug;36(2):345–349. doi: 10.1099/0022-1317-36-2-345. [DOI] [PubMed] [Google Scholar]
- Tatman J. D., Preston V. G., Nicholson P., Elliott R. M., Rixon F. J. Assembly of herpes simplex virus type 1 capsids using a panel of recombinant baculoviruses. J Gen Virol. 1994 May;75(Pt 5):1101–1113. doi: 10.1099/0022-1317-75-5-1101. [DOI] [PubMed] [Google Scholar]
- Telford E. A., Watson M. S., Aird H. C., Perry J., Davison A. J. The DNA sequence of equine herpesvirus 2. J Mol Biol. 1995 Jun 9;249(3):520–528. doi: 10.1006/jmbi.1995.0314. [DOI] [PubMed] [Google Scholar]
- Telford E. A., Watson M. S., McBride K., Davison A. J. The DNA sequence of equine herpesvirus-1. Virology. 1992 Jul;189(1):304–316. doi: 10.1016/0042-6822(92)90706-u. [DOI] [PubMed] [Google Scholar]
- Thomsen D. R., Newcomb W. W., Brown J. C., Homa F. L. Assembly of the herpes simplex virus capsid: requirement for the carboxyl-terminal twenty-five amino acids of the proteins encoded by the UL26 and UL26.5 genes. J Virol. 1995 Jun;69(6):3690–3703. doi: 10.1128/jvi.69.6.3690-3703.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Thomsen D. R., Roof L. L., Homa F. L. Assembly of herpes simplex virus (HSV) intermediate capsids in insect cells infected with recombinant baculoviruses expressing HSV capsid proteins. J Virol. 1994 Apr;68(4):2442–2457. doi: 10.1128/jvi.68.4.2442-2457.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Walker J., Crowley P., Moreman A. D., Barrett J. Biochemical properties of cloned glutathione S-transferases from Schistosoma mansoni and Schistosoma japonicum. Mol Biochem Parasitol. 1993 Oct;61(2):255–264. doi: 10.1016/0166-6851(93)90071-5. [DOI] [PubMed] [Google Scholar]
- Welch A. R., McNally L. M., Gibson W. Cytomegalovirus assembly protein nested gene family: four 3'-coterminal transcripts encode four in-frame, overlapping proteins. J Virol. 1991 Aug;65(8):4091–4100. doi: 10.1128/jvi.65.8.4091-4100.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Welch A. R., McNally L. M., Hall M. R., Gibson W. Herpesvirus proteinase: site-directed mutagenesis used to study maturational, release, and inactivation cleavage sites of precursor and to identify a possible catalytic site serine and histidine. J Virol. 1993 Dec;67(12):7360–7372. doi: 10.1128/jvi.67.12.7360-7372.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Welch A. R., Woods A. S., McNally L. M., Cotter R. J., Gibson W. A herpesvirus maturational proteinase, assemblin: identification of its gene, putative active site domain, and cleavage site. Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10792–10796. doi: 10.1073/pnas.88.23.10792. [DOI] [PMC free article] [PubMed] [Google Scholar]