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PubMed1998

An insect picorna-like virus, Plautia stali intestine virus, has genes of capsid proteins in the 3' part of the genome.

The complete genome of an insect picorna-like virus, Plautia stali intestine virus (PSIV), was cloned and sequenced. The genome had 8797 nucleotides including two consecutive long open reading frames. The deduced amino acid sequence of the first open reading frame (nucleotides 571 to 6003) contained conserved sequence motifs for picornavirus RNA helicase, cysteine protease, and RNA-dependent RNA polymerase. The order of the three motifs in the genome was the same as those of mammalian picornaviruses. The coding regions of four capsid proteins (33, 30, 26, and 4.5 kDa) were mapped by determining their N-terminal sequences. Unlike mammalian picornaviruses, the genes for these proteins were in the 3' region of the PSIV genome. In vitro translation assay suggested that the capsid protein precursor of PSIV would be translated by internal initiation. The deduced amino acid sequence of the capsid proteins showed homology to those of the proteins encoded in the 3' part of the genomes of widely distributed insect picorna-like viruses, cricket paralysis virus, and Drosophila C virus. Some insect picorna-like viruses would have the same unique coding strategy as PSIV.

Amino Acid Sequence↗
PubMed1993

Cloning and nucleotide sequence of the capsid protein and the nuclear inclusion protein (NIb) of potato virus A.

The sequence of the 3'-terminal 2597 nucleotides of potato virus A (PVA) genome has been determined from cDNA clones. An open reading frame was identified and potentially encodes a large polyprotein containing 789 amino acid residues. This large open reading frame was found to have a high similarity to the nuclear inclusion protein (NIb) and the capsid protein (CP) genes of several potyviruses. The data suggest that the PVA NIb and CP are products arising from the maturation of the large polyprotein as observed for other potyviruses. Putative cleavage sites corresponded to consensus sequences NIa/NIb and NIb/CP, respectively, of other potyviruses. The NIb (putative RNA polymerase) and CP are expected to be 516 and 269 amino acid residues (M(r) of 58,939 and 30,094), respectively. The non-coding region is 227 nucleotides long, rich in A and U and unlike other viruses. Furthermore, there are two AUG codons in frame in front of the capsid protein gene suggesting an alternative mode for the capsid protein expression.

Amino Acid Sequence↗
PubMed1989

Cloning of the gene for the capsid protein of potato leafroll virus.

DNA complementary to the RNA of purified potato leafroll virus (PLRV) was synthesized and cloned into the lambda insertion vector NM1149. Overlapping PLRV-specific cDNA clones were isolated that represent some 80% of the viral genome. Sequences coding for the capsid protein were identified by subcloning size-selected cDNAs into the lambda expression vector gt11 and screening with PLRV-specific antisera. The gene for the viral capsid protein was shown to reside in the 3' terminal half of the genomic RNA. Sequence comparisons with the recently published genomes of the beet western yellows virus (BWYV) and the barely yellow dwarf virus (BYDV) reveal some 65% protein sequence homology between the capsid proteins of BWYV and PLRV and some 45% homology between BYDV and PLRV. Furthermore, it is evident that the structural organization of the PLRV genome in the CP gene region is similar to that of BWYV and BYDV.

Amino Acid Sequence↗
PubMed1992

A comparison of the structural polypeptides of three iridescent viruses (types 6, 9, and 16) and the mapping of the DNA region coding for their major capsid polypeptides.

The iridoviruses from Wiseana cervinata (WIV, type 9), Costelytra zealandica (CzIV, type 16) and Chilo suppressalis (CIV, type 6) were compared by SDS-PAGE and Western protein blotting for antigenic determinants. The major capsid proteins were isolated and oligonucleotide probes were synthesized from the partial amino acid sequences. The DNA regions coding for the major capsid proteins of WIV (VP52), CzIV (VP53) and CIV (VP50) were located by hybridization of the oligonucleotide probes to blots of the viral DNA. The major capsid protein was used as the zero point for the proposed linearized maps of these viruses. Using antibody and 125I-labelling, several proteins were identified as being on the surface of the virion. It was also shown that CIV was not as antigenically distinct from these two viruses as previously reported.

Animals↗
PubMedDate not supplied

HIV-1 protease regulation: the role of the major homology region and adjacent C-terminal capsid sequences.

The maturation of human immunodeficiency type-1 virions is accomplished through the proteolytic processing of Gag and GagPol precursor proteins by the viral protease (PR). Since virions must be assembled at the cell surface from uncleaved precursor molecules, intracellular activation of PR must be inhibited. We have previously developed a system where the intracellular activity of PR, associated with GagPol, was inhibited by the expression of Gag in trans. The disproportionate synthesis of Gag inhibits the activation of PR in the cytoplasm. Sequences capable of mediating this inhibition were localized to capsid. In this communication, the region of HIV-1 capsid capable of mediating inhibition was further defined and shown to require the major homology region of capsid within Gag.

Amino Acid Sequence↗
PubMed2004

Three-dimensional structure determination of capsid of Aedes albopictus C6/36 cell densovirus.

The three-dimensional structure of capsid of Aedes albopictus C6/36 densovirus was determined to 14-A resolution by electron cryomicroscopy and computer reconstruction. The triangulation number of the capsid is 1. There are 12 holes in each triangular face and a spike on each 5-fold vertex. The validity of the capsid and nucleic acid densities in the reconstructions was discussed.

Aedes↗
PubMed2006

Mutations in the alpha-helix directly C-terminal to the major homology region of human immunodeficiency virus type 1 capsid protein disrupt Gag multimerization and markedly impair virus particle production.

The X-ray crystallographic structure of HIV-1 capsid protein suggests that the dimer interface of the dimerization domain is mainly formed from a putative alpha-helix structure of 14 amino acids (Gag residues 311-324) and lies directly C-terminal to the capsid major homology region. We found that a deletion mutation in the alpha-helix drastically reduces virus particle production. Alanine-scanning mutagenetic analysis indicated that substitution mutations at residues Q311, V313, K314, W316, and M317 all impair virus particle production markedly. Membrane flotation assays suggested that some mutations in the dimer interface have slight effects on the efficient binding of Gag to membranes. Indirect immunofluorescence studies revealed that mutants defective in virus production exhibit a subcellular distribution pattern similar to that of wild-type. However, velocity sedimentation analysis showed that mutations significantly impairing virus particle production were also detrimental to Gag multimerization, suggesting that the impaired virus production may be due to a defect in Gag multimerization. These results support the proposal that residues in the capsid dimer interface play a crucial role in promoting Gag multimerization, possibly by facilitating stable Gag-Gag interactions.

Capsid Proteins↗
PubMed1977

Optical and hydrodynamic studies of the structure of bacteriophage f2. II. Fluorescence of the capsid.

Fluorescence properties of the icosahedral RNA virus bacteriophage f2 and its empty capsid are reported. Emission is dominated by tryptophan with a maximum wavelength of 320 nm for f2 and its empty capsid. In addition to this short wavelength maximum, perturbation and denaturation studies indicate the inaccessibility of the tryptophan residues. However a high degree of thermal quenching and a red shift in fluorescence emission on heating suggest a noncooperative structural transition, not a denaturation, which allows buried tryptophans to become exposed to solvent. Therefore the tryptophan residues may be located between subunits. Fluorescence from tyrosine is detected near 315 nm for both f2 and its empty capsid, and may indicate an unusual tyrosine environment. Sensitization of tryptophan fluorescence by tyrosine absorption and low values of polarization indicate tyrosine leads to tryptophan and tryptophan leads to tryptophan energy transfer. The presence of RNA in f2 decreases the efficiency of these transfer processes, but does not significantly affect the other reported fluorescence properties.

Capsid↗
PubMed1989

Structure and inherent properties of the bacteriophage lambda head shell. VI. DNA-packaging-defective mutants in the major capsid protein.

Some amino acid substitutions in the major capsid protein (gene E product) of lambda phage are found to cause a defect in DNA packaging. These substitutions permit initiation of DNA packaging and expansion of the prohead. However, cleavage of the concatemer DNA at the cos site takes place only to a very small extent, and the capsid eventually becomes empty. Interestingly, the mutations are suppressed by a decrease of the DNA length between the cos sites by 8000 to 10,000 bases. These properties are similar to those of amber mutants in gene D, which codes for the capsid outer-surface protein. Studies on the E missense.D amber double mutant show that the E protein and the D protein contribute additively to the stabilization of the condensed form of the DNA molecule in phage heads.

Bacteriophage lambda↗
PubMed1989

Synthesis of the capsid protein inhibits development of bacteriophage T3 mutants that abortively infect F plasmid-containing cells.

Mutants of bacteriophage T3 that lack gene 1.2 resemble wild-type phage T7 in that they are unable productively to infect F plasmid-containing cells of Escherichia coli. Pseudorevertants of a T3 gene 1.2 deletion mutant that have regained the ability to plate efficiently on male cells have been isolated and characterized. At least two mutations in the gene for the major capsid protein are necessary for these phages to bypass F-mediated restriction. One mutation serves to reduce the rate of synthesis of the capsid protein; a second mutation apparently alters an unknown property that is intrinsic to the free, or unassembled form of the protein. During the abortive infection of an F-containing host, synthesis of the wild-type capsid protein directly inhibits further phage development.

Capsid↗
PubMed1995

Detection of rabbit haemorrhagic disease virus isolates and sequence comparison of the N-terminus of the capsid protein gene by the polymerase chain reaction.

At present there is no sensitive method for the detection of rabbit haemorrhagic disease virus (RHDV), a calicivirus causing high mortality in rabbit populations. For this purpose a reverse transcriptase polymerase chain reaction (RT-PCR) was established in the N-terminal portion of the RHDV capsid region. The RT-PCR was 10(4)-fold more sensitive than ELISA testing for the detection of the virus and was able to detect as few as 12 copies of template cDNA. By using the RT-PCR test and sequencing, 96.6 to 98.7 per cent homology was demonstrated in the N-terminal portion of the capsid protein of three isolates from geographically and temporally separate outbreaks of viral haemorrhagic disease, indicating that this portion of the RHDV capsid protein is highly conserved.

Amino Acid Sequence↗
PubMed1984

Characterisation of a herpes simplex virus type 1 mutant which has a temperature-sensitive defect in penetration of cells and assembly of capsids.

A herpes simplex virus type 1 (HSV-1) mutant, ts1204, which has a temperature-sensitive (ts) mutation located within genome map coordinates 0.318 to 0.324, close to but outside the coding sequences of the glycoprotein gB gene, has been characterised. Although this mutant adsorbed to the cell surface at the nonpermissive temperature (NPT), it failed to penetrate the cell membrane. As a consequence of this defect, high multiplicities of infection of ts1204 blocked subsequent infection of cells by wild-type HSV-1. By contrast, at the NPT, superinfection of cells with HSV-2 was not inhibited by prior infection with ts1204. The penetration defect could be overcome either by brief incubation of mutant virus-infected cells at the permissive temperature, or by treatment of the cells with polyethylene glycol, a compound which promotes fusion of membranes. Upon continued incubation of ts1204-infected cells at the NPT, low numbers of capsids were assembled. Although these capsids all had some internal structure, they did not contain DNA. Another mutant, ts1208, which lies in the same complementation group as ts1204, penetrated cells normally at the NPT, but like ts1204, had a defect in the formation of functional capsids. Evidence presented in this paper suggests that the gene in which the ts1204 and ts1208 lesions map encodes a structural polypeptide.

Animals↗
PubMed1986

Biochemistry and pathogenicity of echovirus 9. II. Mutants of echovirus 9, strain Hill, with altered capsid surface properties.

The two echovirus 9 strains Hill and Barty have been shown previously not only to differ in pathogenicity for newborn mice but also in a number of in vitro characteristics which depend on viral capsid structure. Three spontaneously occurring mutants of the mouse-apathogenic echovirus 9 prototype strain Hill being resistant to an inhibitor of plaque formation present in agar were isolated and compared biochemically and biophysically to their parent strain and to the mouse-pathogenic echovirus 9 strain Barty, which is resistant to this inhibitor. The mutants differ from their apathogenic parent strain Hill in most of the same in vitro characteristics as strain Barty, namely adsorption to cells in culture, sedimentation behavior in low salt sucrose gradients, distribution of mutant virus particles in isoelectric focusing, and antigenic determinants inducing neutralizing antibodies. For two of the three mutants, Ag2 and Ag3, evidence was obtained from fingerprinting that they differ from their parent strain Hill in VP1; thus, the observed in vitro properties may be caused by the change in this capsid protein. All mutants, however, were found to be apathogenic for newborn mice and do not replicate in the tissues of these animals. It is concluded that the observed changes in capsid structure do not covary with virulence.

Adsorption↗
PubMed1989

In vitro and in vivo expression of rubella virus glycoprotein E2: the signal peptide is contained in the C-terminal region of capsid protein.

The 24 subgenomic mRNA of rubella virus (RV) specifies a polyprotein which is post-translationally processed to three structural protein species E1, E2, and capsid. E1 and E2 are membrane glycoproteins forming the virion spikes. In the polyprotein, E2 and E1 are both preceded by stretches of uncharged, mainly nonpolar amino acids which probably function as signal peptides mediating translocation into the endoplasmic reticulum. We have previously shown that translocation of E1 is reinitiated by a signal peptide located in the carboxy-terminus of E2 (Hobman et al., 1988, J. Virol. 62, 4259-4264). A cDNA from RV encoding the entire E2 gene fused to the capsid N-terminus has been constructed, allowing expression of RV E2 in vitro and in vivo. The resulting protein is efficiently translocated into canine pancreatic microsomes and is glycosylated when expressed in vitro. In vivo some of the N-linked sugars are processed to complex types. Cell surface immunofluorescence indicates that RV E2 is transported to the plasma membrane in COS cells. Oligonucleotide-directed mutagenesis was used to create a cDNA lacking 163 nucleotides immediately 5' to the E2 coding region. This deletion mutant failed undergo translocation into microsomes in vitro and was unstable when expressed in COS cells. The results imply that a signal peptide domain for RV E2 is contained in the carboxyl terminus of the capsid.

Animals↗
PubMed1990

Identification of a bluetongue virus serotype 1-specific ovine helper T-cell determinant in outer capsid protein VP2.

Ovine T-cell lines (including one clone [101A]), which are specific for Bluetongue virus serotype 1 (BTV1), have been established and characterized. Although these T-cell lines react with different isolates of BTV1 (including those from South Africa, Australia, Nigeria, and Cameroon), they do not react with heterologous BTV serotypes. Antigen specificity of these T-cells was studied using purified virus particles, infectious subviral particles (ISVP) and cores, or using individual BTV structural proteins that were either isolated by SDS-PAGE or expressed by recombinant strains of vaccinia virus. The results showed that each of the T-cell lines reacted with outer capsid protein VP2 (the BTV protein exhibiting most serotype-specific variation and the major neutralization antigen). However, all of the uncloned T-cell lines also reacted with either the core structural proteins or the outer capsid protein VP5. In contrast, the T-cell clone 101A only reacted with outer capsid protein VP2. Cell surface marker analysis showed that 101A has a helper T-cell phenotype (CD5+, CD4+, CD8-, T-19-). The T-cell lines and clone 101A all produced large amounts of interleukin 2 (IL-2) when stimulated with purified BTV1 virus particles, or with VP2 (up to 120 IU/ml from 2 x 10(5) T-cells). BTV serotype-specific antigenic sites, for B cells and at least one site for ovine helper T-cells, are therefore located within VP2.

Animals↗
PubMed1991

Point mutations in the turnip crinkle virus capsid protein affect the symptoms expressed by Nicotiana benthamiana.

In an effort to determine the biological function(s) of the capsid protein protruding domains unique to the plant carmo- and tombusviruses, we constructed turnip crinkle virus (TCV) mutants in which tandem, in-frame translation terminators replaced the first two codons of the five-amino acid hinge between the shell and the protruding domains of the TCV capsid protein. One of the mutants replicated in inoculated leaves and protoplasts without detectable accumulation of capsid protein. The mutant lacked the capacity to move systemically in Brassica campestris and Nicotiana benthamiana. After 8 weeks, revertant virions that had regained the capacity to move systemically were purified and found to have sense codons at the positions of the introduced translation terminators. One of the revertants, with amino acid substitutions in the hinge, elicited milder symptoms than those elicited by the wild-type virus, and another elicited more severe symptoms. Oligonucleotide-directed mutagenesis was used to show that the hinge mutations were sufficient to elicit the milder, but not the more severe, symptom syndrome. Single amino acid substitutions were also shown to be sufficient to elicit the milder, but not the more severe, symptoms.

Amino Acid Sequence↗
PubMed1991

Adeno-associated viruses having nonsense mutations in the capsid genes: growth in mammalian cells containing an inducible amber suppressor.

When an adeno-associated virus (AAV) genome contained in a recombinant plasmid is transfected into adenovirus-infected cells, infectious AAV particles are efficiently generated. We previously described the construction of a conditional lethal mutant of AAV having an amber termination codon inserted in the rep gene. This mutant was propagated on a monkey kidney cell line (SupD12) having an inducible amber suppressor tRNAser. We now describe the construction and propagation of two additional conditional lethal mutants of AAV having amber codons affecting all three capsid proteins (AAV Capam) or only the VP1 capsid protein (AAV VP1am). Suppression of the amber mutations in the capsid proteins was demonstrated directly by immunoblot analysis. The efficiency of amber suppression on the SupD12 cell was about 6 to 10% for AAV VP1am and 4 to 5% for AAV Capam. The reversion frequency of either mutant was apparently less than 10(-5). On nonsuppressing cells AAV VP1am exhibited an Lip (Inf) phenotype, whereas AAV Capam exhibited a Cap phenotype.

Animals↗