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Heat-shock protein induction in adriamycin and picornavirus-infected cardiocytes.

BACKGROUND: Both chemicals, such as the chemotherapy agent adriamycin, and viruses, such as the picornaviruses coxsackievirus B3 and encephalomyocarditis virus, cause metabolic injury in myocardial cells. This injury includes depression of cellular RNA and protein synthesis and production of oxygen free radicals which are known to induce increased expression of "heat-shock" or stress proteins (hsp). These hsp can stimulate potent T lymphocyte responses that may then contribute to cardiac damage associated with adriamycin therapy and picornavirus infections. EXPERIMENTAL DESIGN: To determine whether adriamycin and the picornaviruses stimulate hsp expression, cultured neonatal myocardial cells from BALB/c Cum mice were treated with heat-shock, adriamycin and either infectious or ultraviolet irradiated (noninfectious) CVB3. The treated myocardial cell homogenates were subjected to polyacrylamide gel electrophoresis and Western blot analysis for 70 kilodalton hsp. To determine whether these treatments stimulated T lymphocyte responses (presumably to hsp), BALB/c Cum mice were injected with 0.1 ml complete Freund's adjuvant containing 0.1 mg of heat-killed mycobacterium tuberculosis, 10 mg/kg adriamycin or 5 x 10(4) plaque-forming units CVB3 intraperitoneally. Splenic lymphocytes obtained 7 days later from these animals were evaluated in a 51Cr release cytotoxicity assay to cultured myocytes treated with heat-shock, adriamycin or virus. Cytolytic T lymphocytes (CTL) were characterized as to T cell subset and T cell receptor (TcR) utilization treating CTL populations with anti-CD4 or anti-CD8 antibodies or with anti-alpha/beta TcR or anti-gamma/delta TcR antibodies. RESULTS: Both adriamycin and infectious virus treatment of myocardial cells stimulated increased hsp expression. Ultraviolet irradiation of the virus prevents virus replication and failed to elicit hsp production in heart cells. Two types of CTL were detected. Animals injected with complete Freund's adjuvant virus, and adriamycin produced CD8+, gamma/delta TcR+ CTL that were not major histocompatibility complex antigen restricted since both CBA (H-2k) and BALB/c (H-2d) myocardial cells were lysed. Virus-specific CTL, belonging to the CD4+, alpha/beta TcR+ population, were detected in CVB3-infected mice. CONCLUSIONS: Different agents that metabolically injure myocardial cells can induce increased expression of one or more hsp. CTL presumably directed to these hsp can cross-reactively lyse targets treated with any of the hsp inducing agents. This observation raises the question whether multiple exposures of individuals to dramatically different hsp-inducing agents might result in increasingly damaging immune responses.

Animals↗

Simultaneous Streptococcus and picornavirus infection. Muscle involvement in acute rhabdomyolysis.

Streptococci seldom invade muscle in healthy people with intact integument. However, infection with another agent simultaneously may change this general observation. In a two-week period we encountered dual infections with group A, beta-hemolytic streptococci and a picornavirus in each of two hospitalized patients. Both were acutely ill; one died. Renal failure developed in the patient who survived and rhabdomyolysis was demonstrated in the patient who died. Picornavirus titer increases were demonstrated in the patient who survived, and viral inclusions in muscle cells were demonstrated by light microscopy in necropsy specimens and confirmed by electron microscopy in the second patient. We believe that streptococcal invasion of muscle may be facilitated during an outbreak of certain picornavirus infections.

Acute Disease↗

Picornaviruses of laboratory and wild Drosophila melanogaster: geographical distribution and serotypic composition.

Picornaviruses were sought in a large number of D. melanogaster strains, coming from laboratories or recently collected from different parts of the world. About a third of these stocks contained viruses. Regions naturally infected were warm countries. Picornaviruses found in laboratories as well as in wild drosophila flies were the already known P and C viruses, of serotype 1 and 2, and a new virus of serotype 3 belonging by its biological properties to the P group. We did not find derological relationship between D. melanogaster and A. mellifera Picornaviruses.

Bees↗

Picornavirus proteins share antigenic determinants with heat shock proteins 60/65.

Immunological cross-reactions between enteroviruses and islet cell autoantigens have been suggested to play a role in the etiopathogenesis of insulin dependent diabetes mellitus (IDDM). In the nonobese diabetic mouse, an autoimmune model of IDDM, one of the reactive beta cell autoantigens is the heat shock protein 60 (HSP60). These studies were prompted by sequence homology discovered between the immunogenic region in HSP60 and two regions in enterovirus capsid proteins, one in the VP1 protein and the other in the VP0, the precursor of VP2 and VP4 proteins. Possible immunological cross-reactions between enterovirus proteins and heat shock proteins were studied by EIA and immunoblotting by using purified virus preparations, viral expression proteins VP1 and VP0, and recombinant HSP60/65 proteins, and corresponding polyclonal antisera. The HSP60/65 family of proteins is highly conserved and there is a striking degree of homology between bacterial and human heat shock proteins. Rabbit antibodies to HSP65 of Mycobacterium bovis that reacted with human HSP60 were also found to recognise capsid protein VP1 of coxsackievirus A9, VP1, and/or VP2 of coxsackievirus B4. Both viruses were also recognised by antisera raised against HSP60 of Chlamydia pneumoniae. In addition to the capsid proteins derived from native virions, antisera to both bacterial HSP proteins recognised expression protein VP1 of coxsackievirus A9. The cross-reactivity was also demonstrated the other way around; antisera to purified virus particles reacted with the HSP 60/65 proteins to some extent. These results suggest that apart from the well-documented sequence homology between the 2C protein of coxsackieviruses and the beta-cell autoantigen glutamic acid decarboxylase, there are other motifs in picornavirus proteins homologous to islet cell autoantigens, which might induce cross-reacting immune responses during picornavirus infections.

Antibodies, Bacterial↗

Induction of chemokines in human astrocytes by picornavirus infection requires activation of both AP-1 and NF-kappa B.

Infection with different picornaviruses can cause meningitis/encephalitis in humans and experimental animals. To investigate the mechanisms of such inflammatory diseases, potential chemokine gene activation in human astrocytes was investigated following infection with Theiler's murine encephalomyelitis virus (TMEV), coxsackievirus B3 (CVB3), or coxsackievirus B4 (CVB4). We report that all these viruses are potent inducers for the expression of interleukin-8 (IL-8) and monocyte chemoattractant protein-1 (MCP-1) genes in primary human astrocytes, as well as in an established astrocyte cell line (U-373MG). Further studies indicated that both activator protein-1 (AP-1) and NF-kappaB transcription factors are required in the activation of chemokine genes in human astrocytes infected with various picornaviruses. Interestingly, the pattern of activated chemokine genes in human astrocytes is quite restricted compared to that in mouse astrocytes infected with the same viruses, suggesting species differences in gene activation. This may result in potential differences in the pathogenic outcome in each species.

Animals↗

Is Sindbis a simple picornavirus with an envelope?

A three-dimensional image reconstruction was performed from cryo-electron micrographs of isolated Sindbis (SNV) nucleocapsids. The isolated capsid is a smooth but fenestrated T = 3 structure. Comparison with the nucleocapsid seen within the whole virion indicated that the structure resembles the swollen forms which some non-enveloped viruses adopt after removal of divalent cations. A sensitive comparison method was used to align SNV capsid protein sequences with those of picornavirus vp3 capsid proteins whose high resolution structures display an eight-stranded beta-barrel fold found in many icosahedral viruses. The alignment predicted a similar folding for the Sindbis protein which juxtaposes several sets of residues known to be essential for its serine proteolytic activity. These results suggest that the capsid proteins of the enveloped alphaviruses and the non-enveloped picornaviruses may have arisen through divergent evolution from a simple, vp3-like ancestor.

Amino Acid Sequence↗

A new picornavirus isolated from bank voles (Clethrionomys glareolus).

A previously unknown picornavirus was isolated from bank voles (Clethrionomys glareolus). Electron microscopy images and sequence data of the prototype isolate, named Ljungan virus, showed that it is a picornavirus. The amino acid sequences of predicted Ljungan virus capsid proteins VP2 and VP3 were closely related to the human pathogen echovirus 22 (approximately 70% similarity). A partial 5' noncoding region sequence of Ljungan virus showed the highest degree of relatedness to cardioviruses. Two additional isolates were serologically and molecularly related to the prototype.

Amino Acid Sequence↗

The complete genome sequence of Perina nuda picorna-like virus, an insect-infecting RNA virus with a genome organization similar to that of the mammalian picornaviruses.

Perina nuda picorna-like virus (PnPV) is an insect-infecting RNA virus with morphological and physicochemical characters similar to the Picornaviridae. In this article, we determine the complete genome sequence and analyze the gene organization of PnPV. The genome of PnPV consists of 9476 nucleotides (nts) excluding the poly(A) tail and contains a single large open reading frame (ORF) of 8958 nts (2986 codons) flanked by 473 and 45 nt noncoding regions on the 5' and 3' ends, respectively. Northern blotting did not detect the presence of any subgenomic RNA. The PnPV genome codes for four structural proteins (CP1-4), and determination of their N-terminal sequences by Edman degradation, showed that all four are located in the 5' region of the genome. The 3' part of the PnPV genome contains the consensus sequence motifs for picornavirus RNA helicase, cysteine protease, and RNA-dependent RNA polymerase (RdRp) in that order from the 5' to the 3' end. In all of these characters, the genome organization of PnPV resembles the mammalian picornaviruses and two other insect picorna-like viruses, infectious flacherie virus (IFV) of the silkworm and Sacbrood virus (SBV) of the honeybee. In a phylogenetic tree based on the eight conserved domains in the RdRp sequence, PnPV formed a separate cluster with IFV and SBV, which suggests that these three insect picorna-like viruses might constitute a novel group of insect-infecting RNA viruses.

Amino Acid Sequence↗

A common structural core in the internal ribosome entry sites of picornavirus, hepatitis C virus, and pestivirus.

Cap-independent translations of viral RNAs of enteroviruses and rhinoviruses, cardioviruses and aphthoviruses, hepatitis A and C viruses (HAV and HCV), and pestivirus are initiated by the direct binding of 40S ribosomal subunits to a cis-acting genetic element termed the internal ribosome entry site (IRES) or ribosome landing pad (RLP) in the 5' noncoding region (5'NCR). RNA higher ordered structure models for these IRES elements were derived by a combined approach using thermodynamic RNA folding, Monte Carlo simulation, and phylogenetic comparative analysis. The structural differences among the three groups of picornaviruses arise not only from point mutations, but also from the addition or deletion of structural domains. However, a common core can be identified in the proposed structural models of these IRES elements from enteroviruses and rhinoviruses, cardioviruses and aphthoviruses, and HAV. The common structural core identified within the picornavirus IRES is also conserved in the 5'NCR of the divergent viruses, HCV, and pestiviruses. Furthermore, the proposed structural motif shares a structural feature similar to that observed in the catalytic core of the group 1 intron. The conserved structural motif from these divergent sequences that looks like the common core region of group 1 introns is probably a crucial element involved in the IRES-dependent translation.

Animals↗

Molecular cloning and sequencing of coat protein-encoding cDNA of rice tungro spherical virus--a plant picornavirus.

Rice tungro spherical virus (RTSV) was shown to have three coat protein (CP) species by high resolution NaDodSO4-PAGE and Western blot analyses. The sequence of a coat protein-expressing cDNA clone that was identified and selected from a RTSV cDNA library showed that the insert was composed of 2823 bp with only one large open reading frame (ORF) coding for 941 amino acids. The positions of the three coat proteins were located in the putative polyprotein by N-terminal microsequencing and were shown to start at amino acids 287, 495, and 698 for CP-1, CP-2, and CP-3, respectively. The coat proteins are expressed as a polyprotein at the 5' region of the viral RNA genome, and all are cleaved at glutamine carboxy termini, presumably by picornavirus 3C-type of protease(s). Sequence comparisons of coat proteins revealed that there are high amino acid homologies between CP-2 of RTSV and VP3s of encephalomyocarditis virus (EMCV) and Theiler's murine encephalomyelitis virus (TMEV). These results indicate that RTSV is a plant picornavirus.

Amino Acid Sequence↗

Conformational changes during proteolytic processing of a picornavirus capsid proteins.

We have used synthetic peptide antibodies to probe conformational changes that occur during the cleavage cascade which generates the capsid proteins of a picornavirus. The initial translation product of 97 kDa, the precursor of all four structural proteins, is cleaved to form a 63 kDa fragment which, we show, has significantly different folding characteristics to both its larger parent and its products. We demonstrate that proteolytic cleavages as distant as 520 residues from epitopes confer sufficiently large conformational changes as to render them unrecognisable. To our knowledge, this is the first demonstration of this phenomenon in the picornavirus system.

Animals↗

Prokaryotic-like cis elements in the cap-independent internal initiation of translation on picornavirus RNA.

Initiation of translation on picornavirus RNAs is accomplished through internal binding of ribosomes to a complex cis-acting element. Here we show that efficient function of this element involves two appropriately spaced smaller elements: UUUCC and an AUG. This conclusion emerged from analysis of the genome structures of spontaneous revertants of mutant polioviruses with extended insertions between the UUUCC and AUG motifs. It was confirmed by the results obtained with specially designed constructs. A similarity to the prokaryotic translation initiation mechanism, which involves the Shine-Dalgarno sequence, is emphasized, but in the picornavirus system the position of the UUUCC must be strictly fixed relative to upstream cis-acting elements, and the AUG may not necessarily serve as an initiation codon.

Base Sequence↗

In vitro and in vivo anti-picornavirus activity of some p-benzoylphenoxypyridines.

Fifteen p-benzoylphenoxypyridines were initially evaluated for their in vitro activity against rhinoviruses (RV) 1A, 2 and 64 and coxsackie virus (Cox) A21 and for their oral prophylactic and therapeutic activity in Swiss albino mice lethally challenged with Cox A21. One compound, (4-[(5-methylsulfonyl-2-pyridinyl)oxy]phenyl) phenyl methanone, was selected for additional evaluation. These studies showed the compound to possess MIC50 values of less than or equal to 5 micrograms/ml against only 6 of 20 (30.0%) RV serotypes tested. In contrast, the compound was active at concentrations of less than or equal to 5.0 micrograms/ml against 10 of 12 (83.3%) enteroviruses evaluated. In vivo studies showed the compound to significantly protect mice lethally infected with Cox A21 after a single oral dose of 37.5 mg/kg (P less than 0.02) and during a regimen of continuous oral doses of at least 4.7 mg/kg per day (P less than 0.001). Mechanism of action studies indicated that the compound inhibits picornavirus uncoating or some earlier virus-host cell-associated event. Isotopic studies show that (4-[(5-methylsulfonyl-2-pyridinyl)oxy]phenyl) phenyl methanone perturbs HeLa cell macromolecular synthesis at concentrations of as low as 3.12 micrograms/ml. This concentration is only 4-fold higher than the concentration of compound necessary to inhibit Cox A21 RNA synthesis by 90%. This narrow therapeutic ratio limits the potential clinical utility of this compound to all but the most serious picornavirus infections.

Animals↗

SDZ 35-682, a new picornavirus capsid-binding agent with potent antiviral activity.

SDZ 35-682 is a potent and selective inhibitor of the replication of members of the picornavirus group. It inhibits several rhinovirus serotypes and echovirus 9 at concentrations as low as 0.1 micrograms/ml, without exerting any effect on cell proliferation up to 30 micrograms/ml. As observed with other capsid-binding antipicornavirus compounds, there is a wide variation in sensitivity of the different serotypes within the rhinovirus group. The point of interference of SDZ 35-682 in a single cycle of virus growth is an early event taking place before 2 or 3 h of echo- or rhinovirus replication, respectively. By incorporation of neutral red into the viral capsid and measurement of acquisition of photoresistance it is shown that uncoating of echovirus 9 is inhibited by SDZ 35-682. In addition, efficiency of adsorption of echovirus 9 is reduced by SDZ 35-682. To demonstrate that SDZ 35-682, like other uncoating inhibitors of picornaviruses, binds to the hydrophobic pocket beneath the canyon floor co-crystallization with HRV 14 was performed. Considerable conformational changes occur in VP1 in the HRV 14/SDZ 35-682 complex. SDZ 35-682 is 19 A long from end to end and thus fills the entire hydrophobic pocket including its innermost end; it is less flexible than other long antiviral agents. It has been suggested that compounds filling the entire hydrophobic pocket will affect the uncoating process of the virion. Thus, inhibition of viral uncoating, as demonstrated with echovirus 9, probably is the predominant mode of action of SDZ 35-682.

Animals↗

A novel and rapid method to quantify cytolytic replication of picornaviruses in cell culture.

Determining viral titers is a key issue in a wide variety of studies regarding different aspects of virology. The standard methods used for determining picornavirus titers are endpoint titration assay and plaque assay, both time consuming and laborious. The method described uses the tetrazolium salt MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium-bromide) that is reduced to formazane by cellular dehydrogenase, genes shown to be down-regulated during picornavirus infection. The amount formazane produced correlates with the viral titers obtained and can easily be measured using an ELISA plate reader. The colorimetric method has been evaluated using virus types from different genera of the Picornaviridae family. The MTT method reduces the time spent on determining the viral titers and still maintains a reliable accuracy.

Animals↗

Disrupted spatial memory is a consequence of picornavirus infection.

Picornaviruses are a socioeconomically important family of viruses that includes the rhinoviruses and enteroviruses. Many of these viruses, including the "common cold" Coxsackie virus A21, maintain neurovirulent potential and may induce hippocampal injury. The behavioral implications of this injury have not been adequately explored. Using C57BL/6J mice infected with Theiler's murine encephalomyelitis virus, we examined the formation of spatial memories using the Morris water maze test. Virus-infected mice had greater search error compared to sham-infected animals during the location of a hidden platform and were unable to discriminate the location of the training quadrant during the final probe trial. Furthermore, sham-infected mice were place responders whereas virus-infected mice were cue responders, indicating a lack of spatial memory formation in infected animals. Importantly, the degree of memory impairment was correlated to the extent of hippocampal injury. This suggests that picornavirus infection of the human CNS may also result in at least some degree of neurologic deficit. An important implication of such subclinical virus-induced neurologic deficit is that the injury may accumulate over the lifetime of the individual, eventually leading to the manifestation of clinical cognitive or memory deficits.

Animals↗

Internal initiation: IRES elements of picornaviruses and hepatitis c virus.

The scanning hypothesis provides an explanation for events preceding the first peptide bond formation during the translation of the vast majority of eukaryotic mRNAs. However, this hypothesis does not explain the translation of eukaryotic mRNAs lacking the cap structure required for scanning. The existence of a group of positive sense RNA viruses lacking cap structures (e.g. picornaviruses) indicates that host cells also contain a 5' cap-independent translation mechanism. This review discusses the translation mechanisms of atypical viral mRNAs such as picornaviruses and hepatitis c virus, and uses these mechanisms to propose a general theme for all translation, including that of both eukaryotic and prokaryotic mRNAs.

Animals↗

Strategy for construction of live picornavirus vaccines.

A number of recombinant viruses between the virulent Mahoney and the attenuated Sabin 1 strains of type 1 poliovirus were constructed in vitro using their infectious cDNA clones. Monkey neurovirulence tests on these recombinant viruses revealed that the surface structure of the virion particle had a little correlation with the neurovirulent phenotype, and that the strong neurovirulence determinant(s) resided in the 5' noncoding sequence. These results in turn led to two possible strategies for constructing live attenuated picornavirus strains. One is to use the Sabin 1 strain as a vector carrying foreign antigenicities. The other is the construction of the attenuated picornaviruses by introducing mutations into the 5' noncoding sequences. The antigenicity of the Sabin 1 strain was successfully changed to those of other poliovirus serotypes without loss of vaccine quality. Furthermore, it was proved that introduction of deletion mutation into the 5' noncoding sequence of genomes of the Sabin 1 and Mahoney strains resulted in construction of viruses with a less neurovirulent phenotype.

Chromosome Deletion↗