The Experts below are selected from a list of 282 Experts worldwide ranked by ideXlab platform
Albert Bosch - One of the best experts on this subject based on the ideXlab platform.
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HepAtitis A Virus VAccine EscApe VAriAnts And PotentiAl New Serotype Emergence
Emerging infectious diseases, 2011Co-Authors: Unai Pérez-sautu, M. Isabel Costafreda, Joan Arthur Caylà, Cecilia Tortajada, Josep Lite, Albert Bosch, Rosa M. PintóAbstract:Six HepAtitis A Virus Antigenic vAriAnts thAt likely escAped the protective effect of AvAilAble vAccines were isolAted, mostly from men who hAve sex with men. The need to complete the proper vAccinAtion schedules is criticAl, pArticulArly in the immunocompromised populAtion, to prevent the emergence of vAccine-escAping vAriAnts.
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HepAtitis A Virus: StAte of the Art
Food and Environmental Virology, 2010Co-Authors: Rosa M. Pintó, M. Isabel Costafreda, Francisco J. Pérez-rodriguez, Lucía D’andrea, Albert BoschAbstract:HepAtitis A is the most common Among All HepAtitis worldwide in spite of An efficient vAccine And improved hygiene. Shellfish-borne outbreAks Are still of mAjor concern cAusing hundreds of cAses And huge economicAl losses in the present context of globAl food trAde. HepAtitis A Virus (HAV) is A unique picornAVirus with mAny differences in its moleculAr biology including both its incApAcity to induce the inhibition of the cellulAr protein synthesis And A highly biAsed And deoptimized codon usAge with respect the cell. The finAl goAl of this intriguing strAtegy seems to be the need for A fine-tuning control of the trAnslAtion kinetics, pArticulArly At the cApsid coding region, And the underlying mechAnism is the use of A right combinAtion of common And rAre codons to Allow A regulAted ribosome trAffic rAte thus ensuring the proper protein folding. CApsid folding is criticAl to wArrAnt A high environmentAl stAbility for A Virus trAnsmitted through the fecAl–orAl route with long extrAcorporeAl periods.
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HepAtitis A Virus
Methods in molecular biology (Clifton N.J.), 2004Co-Authors: Gloria Sánchez, Albert Bosch, C. Villena, Rosa M. PintóAbstract:HepAtitis A Virus (HAV) infection is the leAding cAuse of virAl HepAtitis throughout the world. HAV infection is mAinly propAgAted viA the fecAl-orAl route, And wAterborne And foodborne outbreAks of the diseAse hAve been reported.HAV, the prototype of the genus HepAtoVirus, belongs to the fAmily PicornAviridAe. Its 7.5-kb single-strAnded RNA genome beArs different distinct regions: the 5' And 3' noncoding regions (NCR), the P1 region, which encodes the structurAl proteins VP1, VP2, VP3, And A putAtive VP4, And the P2 And P3 regions encoding nonstructurAl proteins AssociAted with replicAtion. A single HAV serotype hAs been described, Although seven genotypes hAve been defined. Since environmentAl sAmples usuAlly contAin low numbers of virAl pArticles, sensitive methods such As moleculAr techniques bAsed on nucleic Acid AmplificAtion Are required for their detection. However, even with the Adoption of these techniques, the choice of the most AdequAte tArget is of relevAnt importAnce. The tArget region should be highly conserved, to increAse the chAnce of detection, And should hAve An AppropriAte structure And length to Allow sensitivity high enough for these kind of sAmples. As A tArget region, we hAve chosen A frAgment of the 5'NCR flAnked by highly conserved sequences thAt hAve been used for the primer design (forwArd primer from position 68 to position 85; reverse primer from position 222 to position 240 in the HM175 strAin of HAV; GenBAnk Accession number M14707). The internAl pArt of this region, however, mAy present A certAin degree of vAriAtion mAinly owing to insertions And/or deletions, cAusing A vAriAble size of the Amplimer obtAined, i.e., the wild-type HM175 strAin gives A size of 174 bp whereAs the cell-AdApted pHM175 strAin gives A size of 186 bp. For this reAson it is extremely importAnt to include A confirmAtive method such As Southern blot hybridizAtion with An internAl probe from A region not Affected by the insertions/deletions.
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HepAtitis A Virus polyprotein processing by EscherichiA coli proteAses.
Journal of General Virology, 2002Co-Authors: Rosa M. Pintó, Gloria Sánchez, Susana Guix, Juan F. González-dankaart, Santiago Caballero, Ke-jian Guo, Enric Ribes, Albert BoschAbstract:HepAtitis A Virus (HAV) encodes A single polyprotein, which is post-trAnslAtionAlly processed. This processing represents An essentiAl step in cApsid formAtion. The Virus possesses only one proteAse, 3C, responsible for All cleAvAges, except for thAt At the VP1/2A junction region, which is processed by cellulAr proteAses. In this study, dAtA demonstrAtes thAt HAV polyprotein processing by EscherichiA coli proteAse(s) leAds to the formAtion of pArticulAte structures. P3 polyprotein processing in E. coli is not dependent on An Active 3C proteAse: the sAme processing pAttern is observed with wild-type 3C or with severAl 3C mutAnts. However, this processing pAttern is temperAture-dependAnt, since it differs At 37 or 42 ∞C. The bActeriAl proteAse(s) cleAve scissile bonds other thAn those of HAV; this contributes to the low efficiency of pArticle formAtion.
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HepAtitis A Virus polyprotein processing by EscherichiA coli proteAses.
The Journal of general virology, 2002Co-Authors: Rosa M. Pintó, Gloria Sánchez, Susana Guix, Juan F. González-dankaart, Santiago Caballero, Ke-jian Guo, Enric Ribes, Albert BoschAbstract:HepAtitis A Virus (HAV) encodes A single polyprotein, which is post-trAnslAtionAlly processed. This processing represents An essentiAl step in cApsid formAtion. The Virus possesses only one proteAse, 3C, responsible for All cleAvAges, except for thAt At the VP1/2A junction region, which is processed by cellulAr proteAses. In this study, dAtA demonstrAtes thAt HAV polyprotein processing by EscherichiA coli proteAse(s) leAds to the formAtion of pArticulAte structures. P3 polyprotein processing in E. coli is not dependent on An Active 3C proteAse: the sAme processing pAttern is observed with wild-type 3C or with severAl 3C mutAnts. However, this processing pAttern is temperAture-dependent, since it differs At 37 or 42 degrees C. The bActeriAl proteAse(s) cleAve scissile bonds other thAn those of HAV; this contributes to the low efficiency of pArticle formAtion.
Rosa M. Pintó - One of the best experts on this subject based on the ideXlab platform.
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HepAtitis A Virus VAccine EscApe VAriAnts And PotentiAl New Serotype Emergence
Emerging infectious diseases, 2011Co-Authors: Unai Pérez-sautu, M. Isabel Costafreda, Joan Arthur Caylà, Cecilia Tortajada, Josep Lite, Albert Bosch, Rosa M. PintóAbstract:Six HepAtitis A Virus Antigenic vAriAnts thAt likely escAped the protective effect of AvAilAble vAccines were isolAted, mostly from men who hAve sex with men. The need to complete the proper vAccinAtion schedules is criticAl, pArticulArly in the immunocompromised populAtion, to prevent the emergence of vAccine-escAping vAriAnts.
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HepAtitis A Virus: StAte of the Art
Food and Environmental Virology, 2010Co-Authors: Rosa M. Pintó, M. Isabel Costafreda, Francisco J. Pérez-rodriguez, Lucía D’andrea, Albert BoschAbstract:HepAtitis A is the most common Among All HepAtitis worldwide in spite of An efficient vAccine And improved hygiene. Shellfish-borne outbreAks Are still of mAjor concern cAusing hundreds of cAses And huge economicAl losses in the present context of globAl food trAde. HepAtitis A Virus (HAV) is A unique picornAVirus with mAny differences in its moleculAr biology including both its incApAcity to induce the inhibition of the cellulAr protein synthesis And A highly biAsed And deoptimized codon usAge with respect the cell. The finAl goAl of this intriguing strAtegy seems to be the need for A fine-tuning control of the trAnslAtion kinetics, pArticulArly At the cApsid coding region, And the underlying mechAnism is the use of A right combinAtion of common And rAre codons to Allow A regulAted ribosome trAffic rAte thus ensuring the proper protein folding. CApsid folding is criticAl to wArrAnt A high environmentAl stAbility for A Virus trAnsmitted through the fecAl–orAl route with long extrAcorporeAl periods.
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HepAtitis A Virus
Methods in molecular biology (Clifton N.J.), 2004Co-Authors: Gloria Sánchez, Albert Bosch, C. Villena, Rosa M. PintóAbstract:HepAtitis A Virus (HAV) infection is the leAding cAuse of virAl HepAtitis throughout the world. HAV infection is mAinly propAgAted viA the fecAl-orAl route, And wAterborne And foodborne outbreAks of the diseAse hAve been reported.HAV, the prototype of the genus HepAtoVirus, belongs to the fAmily PicornAviridAe. Its 7.5-kb single-strAnded RNA genome beArs different distinct regions: the 5' And 3' noncoding regions (NCR), the P1 region, which encodes the structurAl proteins VP1, VP2, VP3, And A putAtive VP4, And the P2 And P3 regions encoding nonstructurAl proteins AssociAted with replicAtion. A single HAV serotype hAs been described, Although seven genotypes hAve been defined. Since environmentAl sAmples usuAlly contAin low numbers of virAl pArticles, sensitive methods such As moleculAr techniques bAsed on nucleic Acid AmplificAtion Are required for their detection. However, even with the Adoption of these techniques, the choice of the most AdequAte tArget is of relevAnt importAnce. The tArget region should be highly conserved, to increAse the chAnce of detection, And should hAve An AppropriAte structure And length to Allow sensitivity high enough for these kind of sAmples. As A tArget region, we hAve chosen A frAgment of the 5'NCR flAnked by highly conserved sequences thAt hAve been used for the primer design (forwArd primer from position 68 to position 85; reverse primer from position 222 to position 240 in the HM175 strAin of HAV; GenBAnk Accession number M14707). The internAl pArt of this region, however, mAy present A certAin degree of vAriAtion mAinly owing to insertions And/or deletions, cAusing A vAriAble size of the Amplimer obtAined, i.e., the wild-type HM175 strAin gives A size of 174 bp whereAs the cell-AdApted pHM175 strAin gives A size of 186 bp. For this reAson it is extremely importAnt to include A confirmAtive method such As Southern blot hybridizAtion with An internAl probe from A region not Affected by the insertions/deletions.
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HepAtitis A Virus polyprotein processing by EscherichiA coli proteAses.
Journal of General Virology, 2002Co-Authors: Rosa M. Pintó, Gloria Sánchez, Susana Guix, Juan F. González-dankaart, Santiago Caballero, Ke-jian Guo, Enric Ribes, Albert BoschAbstract:HepAtitis A Virus (HAV) encodes A single polyprotein, which is post-trAnslAtionAlly processed. This processing represents An essentiAl step in cApsid formAtion. The Virus possesses only one proteAse, 3C, responsible for All cleAvAges, except for thAt At the VP1/2A junction region, which is processed by cellulAr proteAses. In this study, dAtA demonstrAtes thAt HAV polyprotein processing by EscherichiA coli proteAse(s) leAds to the formAtion of pArticulAte structures. P3 polyprotein processing in E. coli is not dependent on An Active 3C proteAse: the sAme processing pAttern is observed with wild-type 3C or with severAl 3C mutAnts. However, this processing pAttern is temperAture-dependAnt, since it differs At 37 or 42 ∞C. The bActeriAl proteAse(s) cleAve scissile bonds other thAn those of HAV; this contributes to the low efficiency of pArticle formAtion.
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HepAtitis A Virus polyprotein processing by EscherichiA coli proteAses.
The Journal of general virology, 2002Co-Authors: Rosa M. Pintó, Gloria Sánchez, Susana Guix, Juan F. González-dankaart, Santiago Caballero, Ke-jian Guo, Enric Ribes, Albert BoschAbstract:HepAtitis A Virus (HAV) encodes A single polyprotein, which is post-trAnslAtionAlly processed. This processing represents An essentiAl step in cApsid formAtion. The Virus possesses only one proteAse, 3C, responsible for All cleAvAges, except for thAt At the VP1/2A junction region, which is processed by cellulAr proteAses. In this study, dAtA demonstrAtes thAt HAV polyprotein processing by EscherichiA coli proteAse(s) leAds to the formAtion of pArticulAte structures. P3 polyprotein processing in E. coli is not dependent on An Active 3C proteAse: the sAme processing pAttern is observed with wild-type 3C or with severAl 3C mutAnts. However, this processing pAttern is temperAture-dependent, since it differs At 37 or 42 degrees C. The bActeriAl proteAse(s) cleAve scissile bonds other thAn those of HAV; this contributes to the low efficiency of pArticle formAtion.
Gloria Sánchez - One of the best experts on this subject based on the ideXlab platform.
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HepAtitis A Virus
Methods in molecular biology (Clifton N.J.), 2004Co-Authors: Gloria Sánchez, Albert Bosch, C. Villena, Rosa M. PintóAbstract:HepAtitis A Virus (HAV) infection is the leAding cAuse of virAl HepAtitis throughout the world. HAV infection is mAinly propAgAted viA the fecAl-orAl route, And wAterborne And foodborne outbreAks of the diseAse hAve been reported.HAV, the prototype of the genus HepAtoVirus, belongs to the fAmily PicornAviridAe. Its 7.5-kb single-strAnded RNA genome beArs different distinct regions: the 5' And 3' noncoding regions (NCR), the P1 region, which encodes the structurAl proteins VP1, VP2, VP3, And A putAtive VP4, And the P2 And P3 regions encoding nonstructurAl proteins AssociAted with replicAtion. A single HAV serotype hAs been described, Although seven genotypes hAve been defined. Since environmentAl sAmples usuAlly contAin low numbers of virAl pArticles, sensitive methods such As moleculAr techniques bAsed on nucleic Acid AmplificAtion Are required for their detection. However, even with the Adoption of these techniques, the choice of the most AdequAte tArget is of relevAnt importAnce. The tArget region should be highly conserved, to increAse the chAnce of detection, And should hAve An AppropriAte structure And length to Allow sensitivity high enough for these kind of sAmples. As A tArget region, we hAve chosen A frAgment of the 5'NCR flAnked by highly conserved sequences thAt hAve been used for the primer design (forwArd primer from position 68 to position 85; reverse primer from position 222 to position 240 in the HM175 strAin of HAV; GenBAnk Accession number M14707). The internAl pArt of this region, however, mAy present A certAin degree of vAriAtion mAinly owing to insertions And/or deletions, cAusing A vAriAble size of the Amplimer obtAined, i.e., the wild-type HM175 strAin gives A size of 174 bp whereAs the cell-AdApted pHM175 strAin gives A size of 186 bp. For this reAson it is extremely importAnt to include A confirmAtive method such As Southern blot hybridizAtion with An internAl probe from A region not Affected by the insertions/deletions.
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HepAtitis A Virus polyprotein processing by EscherichiA coli proteAses.
Journal of General Virology, 2002Co-Authors: Rosa M. Pintó, Gloria Sánchez, Susana Guix, Juan F. González-dankaart, Santiago Caballero, Ke-jian Guo, Enric Ribes, Albert BoschAbstract:HepAtitis A Virus (HAV) encodes A single polyprotein, which is post-trAnslAtionAlly processed. This processing represents An essentiAl step in cApsid formAtion. The Virus possesses only one proteAse, 3C, responsible for All cleAvAges, except for thAt At the VP1/2A junction region, which is processed by cellulAr proteAses. In this study, dAtA demonstrAtes thAt HAV polyprotein processing by EscherichiA coli proteAse(s) leAds to the formAtion of pArticulAte structures. P3 polyprotein processing in E. coli is not dependent on An Active 3C proteAse: the sAme processing pAttern is observed with wild-type 3C or with severAl 3C mutAnts. However, this processing pAttern is temperAture-dependAnt, since it differs At 37 or 42 ∞C. The bActeriAl proteAse(s) cleAve scissile bonds other thAn those of HAV; this contributes to the low efficiency of pArticle formAtion.
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HepAtitis A Virus polyprotein processing by EscherichiA coli proteAses.
The Journal of general virology, 2002Co-Authors: Rosa M. Pintó, Gloria Sánchez, Susana Guix, Juan F. González-dankaart, Santiago Caballero, Ke-jian Guo, Enric Ribes, Albert BoschAbstract:HepAtitis A Virus (HAV) encodes A single polyprotein, which is post-trAnslAtionAlly processed. This processing represents An essentiAl step in cApsid formAtion. The Virus possesses only one proteAse, 3C, responsible for All cleAvAges, except for thAt At the VP1/2A junction region, which is processed by cellulAr proteAses. In this study, dAtA demonstrAtes thAt HAV polyprotein processing by EscherichiA coli proteAse(s) leAds to the formAtion of pArticulAte structures. P3 polyprotein processing in E. coli is not dependent on An Active 3C proteAse: the sAme processing pAttern is observed with wild-type 3C or with severAl 3C mutAnts. However, this processing pAttern is temperAture-dependent, since it differs At 37 or 42 degrees C. The bActeriAl proteAse(s) cleAve scissile bonds other thAn those of HAV; this contributes to the low efficiency of pArticle formAtion.
Stanley M. Lemon - One of the best experts on this subject based on the ideXlab platform.
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CompArAtive PAthology of HepAtitis A Virus And HepAtitis E Virus Infection.
Cold Spring Harbor perspectives in medicine, 2019Co-Authors: John M. Cullen, Stanley M. LemonAbstract:HepAtitis A Virus (HAV) And HepAtitis E Virus (HEV) cAuse Acute, self-limiting hepAtic infections thAt Are usuAlly spreAd by the fecAl-orAl route in humAns. NAturAlly occurring And experimentAl infections Are possible in A vAriety of nonhumAn primAtes And, in the cAse of HEV, A number of other species. MAny AdvAnces in understAnding the pAthogenesis of these Viruses hAve come from studies in experimentAl AnimAls. In generAl, AnimAls infected with these Viruses recApitulAte the histologic lesions seen in infected humAns, but typicAlly with less severe clinicAl And histopAthologicAl mAnifestAtions. This review describes the histopAthologic chAnges AssociAted with HAV And HEV infection in humAns And experimentAl AnimAls.
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HepAtitis A Virus Genome OrgAnizAtion And ReplicAtion StrAtegy
Cold Spring Harbor perspectives in medicine, 2018Co-Authors: Kevin L. Mcknight, Stanley M. LemonAbstract:HepAtitis A Virus (HAV) is A positive-strAnd RNA Virus clAssified in the genus HepAtoVirus of the fAmily PicornAviridAe It is An Ancient Virus with A long evolutionAry history And multiple feAtures of its cApsid structure, genome orgAnizAtion, And replicAtion cycle thAt distinguish it from other mAmmAliAn picornAViruses. HAV proteins Are produced by cAp-independent trAnslAtion of A single, long open reAding frAme under direction of An inefficient, upstreAm internAl ribosome entry site (IRES). Genome replicAtion occurs slowly And is noncytopAthic, with trAnscription likely primed by A uridylAted protein primer As in other picornAViruses. Newly produced quAsi-enveloped virions (eHAV) Are releAsed from cells in A nonlytic fAshion in A unique process mediAted by interActions of cApsid proteins with components of the host cell endosomAl sorting complexes required for trAnsport (ESCRT) system.
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HepAtitis A Virus from discovery to vAccines
Hepatology, 2006Co-Authors: Annette Martin, Stanley M. LemonAbstract:HepAtitis A Virus (HAV), the cAusAtive Agent of type A virAl HepAtitis, is An Ancient humAn Virus thAt wAs first identified Almost 35 yeArs Ago. It hAs severAl chArActeristics thAt mAke it unique Among the PicornAviridAe, pArticulArly in terms of its mechAnisms of polyprotein processing And virion morphogenesis, And which likely contribute to its pAthobiology. Although efficAcious vAccines contAining formAlin-inActivAted Virus produced in cell culture hAve been licensed in multiple countries, their use hAs been limited by cost considerAtions. ChAnges in public heAlth sAnitAtion And generAlly increAsing stAndArds of living Are leAding to A decreAsing incidence of Acute HepAtitis A worldwide, with the result thAt the prevAlence of preexisting immunity Among Adults is declining in mAny regions. These chAnges in the epidemiology of HAV mAy pArAdoxicAlly enhAnce the diseAse burden, As greAter numbers of individuAls become infected At older Ages when diseAse is more likely to be clinicAlly evident, thus providing greAter incentives for vAccine utilizAtion.
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The MoleculAr Biology of HepAtitis A Virus
Hepatitis Viruses, 2002Co-Authors: Annette Martin, Stanley M. LemonAbstract:HepAtitis A Virus (HAV) is A positive-strAnd RNA Virus clAssified within the fAmily PicornAviridAe. The mAture HAV virion is A smAll 27 nm, generAlly sphericAl, non-enveloped pArticle (1), with three mAjor cApsid proteins encApsidAting A single-strAnded, positive-sense RNA genome About 7.5 kb in length. Although there Are mAny Attributes of the Virus thAt distinguish it from other picornAViruses, HAV shAres A number of feAtures in common with other members of the fAmily PicornAviridAe, pArticulArly those in the genus AphthoVirus (foot And mouth diseAse Virus, FMDV) And genus CArdioVirus (e.g., encephAlomyocArditis Virus, EMCV). Its genomic orgAnizAtion is Also similAr to thAt of All other picornAViruses, including members of the EnteroVirus (e.g., polioVirus) And RhinoVirus generA. In recognition of its distinctive feAtures, however, HAV is clAssified As the type species of A sepArAte genus, the genus HepAtoVirus. An importAnt humAn pAthogen, HAV is A common cAuse of Acute virAl HepAtitis And one of five humAn Viruses typicAlly AssociAted with this diseAse.
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TAxonomic ClAssificAtion of HepAtitis A Virus
Viral Hepatitis and Liver Disease, 1994Co-Authors: Stanley M. Lemon, Betty H. RobertsonAbstract:Recently, A working group recommended thAt HepAtitis A Virus (HAV) be reclAssified within A new genus (HepAtoVirus) of the fAmily PicornAviridAe. Properties which distinguish the hepAtoViruses from other picornAViruses include hepAtotropism, A tendency to estAblish persistent infections in cell cultures, An exceptionAl stAbility to Acid And heAt, And A monotypic Antigenic structure, As well As A unique pAttern of processing of the cApsid protein precursors And the probAble lAck of myristylAtion of VP4. The decision to plAce HAV within A novel genus wAs Also influenced by the extreme genetic distAnce thAt exists between HAV And All other picornAvirAl generA. “Genotypes” of HAV hAve been defined As those strAins shAring > 85% nucleotide sequence identity within A short segment of the genome locAted At the VP1/PX junction. Viruses recovered from humAns comprise four distinct genotypes (I, II, III, And VII), while three other genotypes (IV, V, And VI) Are eAch represented thus fAr by A single simiAn HAV strAin.
Susana Guix - One of the best experts on this subject based on the ideXlab platform.
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HepAtitis A Virus polyprotein processing by EscherichiA coli proteAses.
Journal of General Virology, 2002Co-Authors: Rosa M. Pintó, Gloria Sánchez, Susana Guix, Juan F. González-dankaart, Santiago Caballero, Ke-jian Guo, Enric Ribes, Albert BoschAbstract:HepAtitis A Virus (HAV) encodes A single polyprotein, which is post-trAnslAtionAlly processed. This processing represents An essentiAl step in cApsid formAtion. The Virus possesses only one proteAse, 3C, responsible for All cleAvAges, except for thAt At the VP1/2A junction region, which is processed by cellulAr proteAses. In this study, dAtA demonstrAtes thAt HAV polyprotein processing by EscherichiA coli proteAse(s) leAds to the formAtion of pArticulAte structures. P3 polyprotein processing in E. coli is not dependent on An Active 3C proteAse: the sAme processing pAttern is observed with wild-type 3C or with severAl 3C mutAnts. However, this processing pAttern is temperAture-dependAnt, since it differs At 37 or 42 ∞C. The bActeriAl proteAse(s) cleAve scissile bonds other thAn those of HAV; this contributes to the low efficiency of pArticle formAtion.
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HepAtitis A Virus polyprotein processing by EscherichiA coli proteAses.
The Journal of general virology, 2002Co-Authors: Rosa M. Pintó, Gloria Sánchez, Susana Guix, Juan F. González-dankaart, Santiago Caballero, Ke-jian Guo, Enric Ribes, Albert BoschAbstract:HepAtitis A Virus (HAV) encodes A single polyprotein, which is post-trAnslAtionAlly processed. This processing represents An essentiAl step in cApsid formAtion. The Virus possesses only one proteAse, 3C, responsible for All cleAvAges, except for thAt At the VP1/2A junction region, which is processed by cellulAr proteAses. In this study, dAtA demonstrAtes thAt HAV polyprotein processing by EscherichiA coli proteAse(s) leAds to the formAtion of pArticulAte structures. P3 polyprotein processing in E. coli is not dependent on An Active 3C proteAse: the sAme processing pAttern is observed with wild-type 3C or with severAl 3C mutAnts. However, this processing pAttern is temperAture-dependent, since it differs At 37 or 42 degrees C. The bActeriAl proteAse(s) cleAve scissile bonds other thAn those of HAV; this contributes to the low efficiency of pArticle formAtion.