{"id":20590,"date":"2021-03-22T08:54:55","date_gmt":"2021-03-22T08:54:55","guid":{"rendered":"http:\/\/prrscontrolidiomas.advertis.es\/2-organizacion-del-genoma-y-estructura-del-virus\/"},"modified":"2021-03-26T09:12:04","modified_gmt":"2021-03-26T09:12:04","slug":"organizacion-del-genoma-y-estructura-del-virus","status":"publish","type":"page","link":"https:\/\/prrscontrol.com\/es\/el-virus-prrs\/organizacion-del-genoma-y-estructura-del-virus\/","title":{"rendered":"<span>2<\/span> Organizaci\u00f3n del genoma y estructura del virus"},"content":{"rendered":"<div class=\"wpb-content-wrapper\"><p>[vc_row][vc_column width=\u00bb1\/1&#8243;][vc_column_text el_class=\u00bbintro\u00bb]El genoma del virus del PRRS consiste en una sola cadena no segmentada de <strong>ARN<\/strong> de sentido\u00a0positivo. El ARN est\u00e1 compuesto por al menos diez fragmentos de lectura abierta (ORF por su\u00a0acr\u00f3nimo en ingl\u00e9s) y su tama\u00f1o total es de unas 15 kb.[\/vc_column_text]<div class=\"single_image wpb_content_element align-left  animate image_box_rounded image_zoom \" data-animation=\"fade-in\" data-delay=\"300\"><a href=\"https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Porcentaje-que-representa-cada-ORF-respecto-al-genoma-completo-del-virus-del-PRRS.jpg\" class=\"prettyPhoto\" rel=\"prettyPhoto[image]\"><img loading=\"lazy\" decoding=\"async\" width=\"1400\" height=\"800\" src=\"https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Porcentaje-que-representa-cada-ORF-respecto-al-genoma-completo-del-virus-del-PRRS.jpg\" class=\"attachment-full\" alt=\"\" title=\"Porcentaje-que-representa-cada-ORF-respecto-al-genoma-completo-del-virus-del-PRRS\" srcset=\"https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Porcentaje-que-representa-cada-ORF-respecto-al-genoma-completo-del-virus-del-PRRS.jpg 1400w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Porcentaje-que-representa-cada-ORF-respecto-al-genoma-completo-del-virus-del-PRRS-300x171.jpg 300w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Porcentaje-que-representa-cada-ORF-respecto-al-genoma-completo-del-virus-del-PRRS-768x439.jpg 768w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Porcentaje-que-representa-cada-ORF-respecto-al-genoma-completo-del-virus-del-PRRS-1024x585.jpg 1024w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Porcentaje-que-representa-cada-ORF-respecto-al-genoma-completo-del-virus-del-PRRS-750x429.jpg 750w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Porcentaje-que-representa-cada-ORF-respecto-al-genoma-completo-del-virus-del-PRRS-1140x651.jpg 1140w\" sizes=\"auto, (max-width: 1400px) 100vw, 1400px\" \/><\/a><\/div>[vc_column_text]<strong>Despu\u00e9s de la 5\u2019-UTR<\/strong>, en sentido de la traducci\u00f3n, se encuentran las ORFs 1a y 1b, las\u00a0cuales dan lugar a dos poliproteinas (pp1a y pp1b). Estas, tras su divisi\u00f3n, dan lugar a 14\u00a0<strong>prote\u00ednas no estructurales<\/strong> (nsp por su acr\u00f3nimo en ingl\u00e9s), incluyendo cuatro proteasas, la\u00a0ARN polimerasa ARN-dependiente, la helicasa y una endoribonucleasa.<\/p>\n<p>Estas prote\u00ednas se\u00a0expresan solo durante la replicaci\u00f3n y no forman parte del viri\u00f3n.[\/vc_column_text][vc_column_text]<\/p>\n<p dir=\"ltr\">Continuando en el sentido de la traducci\u00f3n hasta llegar a 3\u2019 encontramos las ORFs de la 2 a la\u00a07 (ORF2a, ORF2b, ORF3, ORF4, ORF5, ORF5a, ORF6 y ORF7), que codifican para las prote\u00ednas\u00a0estructurales menores y mayores:<\/p>\n<ul>\n<li dir=\"ltr\"><strong>Prote\u00ednas estructurales menores<\/strong>: tres N-glicosiladas: GP2a, GP3 y GP4, las\u00a0cuales forman un tr\u00edmero, y una no glicosilada: E o 2b. El complejo trim\u00e9rico,\u00a0solo o mediante la interacci\u00f3n con GP5, es esencial para la infectividad del\u00a0virus. La prote\u00edna E tambi\u00e9n interact\u00faa con el tr\u00edmero y es importante para la\u00a0replicaci\u00f3n y para el tropismo celular del virus.<\/li>\n<li dir=\"ltr\"><strong>Prote\u00ednas estructurales mayores<\/strong>: la mayor glicoprote\u00edna de la envoltura\u00a0(GP5; codificada por la ORF5), la prote\u00edna no glicosilada de la membrana\u00a0(M; codificada por la ORF6) y la prote\u00edna de la nucleoc\u00e1pside (N; codificada\u00a0por la ORF7). La GP5 y la M forman heterod\u00edmeros que son esenciales para\u00a0la formaci\u00f3n del viri\u00f3n y para la infectividad. Adem\u00e1s, recientemente se ha\u00a0descrito una prote\u00edna estructural llamada <strong>ORF5a<\/strong>. Esta prote\u00edna parece ser\u00a0esencial para el <strong>tropismo celular, durante el proceso de replicaci\u00f3n y para la\u00a0viabilidad del viri\u00f3n<\/strong>.<br \/>\nFinalmente, la prote\u00edna N interacciona con el ARN viral\u00a0en el ensamblaje de la part\u00edcula infectiva. Esta prote\u00edna se utiliza ampliamente\u00a0como ant\u00edgeno para los ensayos diagn\u00f3sticos tipo ELISA debido a su\u00a0abundancia y a su capacidad antig\u00e9nica.<\/li>\n<\/ul>\n<p>[\/vc_column_text]<div class=\"single_image wpb_content_element align-left  animate image_box_rounded image_zoom \" data-animation=\"fade-in\" data-delay=\"300\"><a href=\"https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Genoma-del-virus-del-PRRS.jpg\" class=\"prettyPhoto\" rel=\"prettyPhoto[image]\"><img loading=\"lazy\" decoding=\"async\" width=\"1400\" height=\"1116\" src=\"https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Genoma-del-virus-del-PRRS.jpg\" class=\"attachment-full\" alt=\"\" title=\"Genoma-del-virus-del-PRRS\" srcset=\"https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Genoma-del-virus-del-PRRS.jpg 1400w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Genoma-del-virus-del-PRRS-300x239.jpg 300w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Genoma-del-virus-del-PRRS-768x612.jpg 768w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Genoma-del-virus-del-PRRS-1024x816.jpg 1024w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Genoma-del-virus-del-PRRS-750x598.jpg 750w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/Genoma-del-virus-del-PRRS-1140x909.jpg 1140w\" sizes=\"auto, (max-width: 1400px) 100vw, 1400px\" \/><\/a><\/div>[vc_column_text]El ARN del viri\u00f3n sirve como genoma y como ARN mensajero. Por lo tanto, puede codificar\u00a0directamente las prote\u00ednas.<\/p>\n<p>El viri\u00f3n del PRRS es <strong>esf\u00e9rico<\/strong>, de unos 45-80 nm de di\u00e1metro. La nucleoc\u00e1pside, la cual est\u00e1 formada por la prote\u00edna N y el ARN del genoma est\u00e1 rodeada por una envuelta lip\u00eddica.\u00a0Recientemente, mediante estudios de tomograf\u00eda crioelectr\u00f3nica, se ha sugerido que la\u00a0nucleoc\u00e1pside tiene una <strong>forma asim\u00e9trica<\/strong>, en vez de isom\u00e9trica como previamente se\u00a0asum\u00eda.[\/vc_column_text]<div class=\"single_image wpb_content_element align-left  animate image_box_rounded image_zoom \" data-animation=\"fade-in\" data-delay=\"300\"><a href=\"https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/virion.jpg\" class=\"prettyPhoto\" rel=\"prettyPhoto[image]\"><img loading=\"lazy\" decoding=\"async\" width=\"1400\" height=\"1116\" src=\"https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/virion.jpg\" class=\"attachment-full\" alt=\"\" title=\"virion\" srcset=\"https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/virion.jpg 1400w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/virion-300x239.jpg 300w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/virion-768x612.jpg 768w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/virion-1024x816.jpg 1024w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/virion-750x598.jpg 750w, https:\/\/prrscontrol.com\/wp-content\/uploads\/2021\/03\/virion-1140x909.jpg 1140w\" sizes=\"auto, (max-width: 1400px) 100vw, 1400px\" \/><\/a><\/div>[vc_column_text el_class=\u00bbaviso\u00bb]<\/p>\n<hr \/>\n<p style=\"text-align: center;\">\u00a9 Laboratorios Hipra, S.A. 2026. Reservados todos los derechos.<br \/>\nNinguna parte de este sitio web o cualquiera de sus contenidos puede ser reproducida, copiada, modificada o adaptada, sin el consentimiento previo por escrito de HIPRA.<\/p>\n<p>[\/vc_column_text][\/vc_column][\/vc_row][vc_row top_padding=\u00bb30&#8243; row_id=\u00bbreferencias\u00bb][vc_column width=\u00bb1\/1&#8243;]<div class=\"toggle\"><div class=\"toggle-title \"><i class='fa fal fa-book'><\/i>Referencias<\/div><div class=\"toggle-inner\"><p>\n<ul>\n<li>Allende R, Laegreid WW, Kutish GF, Galeota JA, Wills RW, Osorio FA. Porcine reproductive and respiratory syndrome virus: description of persistence in individual pigs upon experimental infection. J Virol. 2000, 74:10834-7.<\/li>\n<li>Allende R, Kutish GF, Laegreid W, Lu Z, Lewis TL, Rock DL, Friesen J, Galeota JA, Doster AR, Osorio FA. Mutations in the genome of porcine reproductive and respiratory syndrome virus responsible for the attenuation phenotype. 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The small envelope protein of porcine reproductive and respiratory syndrome virus possesses ion channel protein-like properties. Virology. 2006, 355:30-43.<\/li>\n<li>Martelli P, Cordioli P, Fallacara F, Gozio S, Terreni M, Cavirani S. A follow up study of recurrent acute PRRS (Atypical PRRS-SAMS) and genetic variations of ORF5. In Proceedings of the 4th International Symposium on Emerging and Re-emerging Pig Diseases, 75-76, 2003, Italy.<\/li>\n<li>Mart\u00edn-Valls GE, Kvisgaard LK, Tello M, Darwich L, Cortey M, Burgara-Estrella AJ, Hern\u00e1ndez J, Larsen LE, Mateu E. Analysis of ORF5 and full-length genome sequences of porcine reproductive and respiratory syndrome virus isolates of genotypes 1 and 2 retrieved worldwide provides evidence that recombination is a common phenomenon and may produce mosaic isolates. J Virol. 2014, 88:3170-81.<\/li>\n<li>Mengeling WL, Lager KM, Vorwald AC. Clinical consequences of exposing pregnant gilts to strains of porcine reproductive and respiratory syndrome (PRRS) virus isolated from field cases of \u201catypical\u201d PRRS. Am J Vet Res. 1998, 59:1540\u20134.<\/li>\n<li>Meulenberg JJ, Petersen-den Besten A, De Kluyver EP, Moormann RJ, Schaaper WM, Wensvoort G. Characterization of proteins encoded by ORFs 2 to 7 of Lelystad virus. Virology. 1995, 206:155-63.<\/li>\n<li>Meulenberg JJ, Petersen den Besten A, de Kluyver E, van Nieuwstadt A, Wensvoort G, Moormann RJ. Molecular characterization of Lelystad virus. Vet Microbiol. 1997, 55:197-202.<\/li>\n<li>Morgan SB, Frossard JP, Pallares FJ, Gough J, Stadejek T, Graham SP, Steinbach F, Drew TW, Salguero FJ. Pathology and virus distribution in the lung and lymphoid tissues of pigs experimentally inoculated with three distinct type 1 prrs virus isolates of varying pathogenicity. Transbound Emerg Dis. 2014. doi: 10.1111\/tbed.12272.<\/li>\n<li>Morgan SB, Graham SP, Salguero FJ, S\u00e1nchez Cord\u00f3n PJ, Mokhtar H, Rebel JM, Weesendorp E, Bodman-Smith KB, Steinbach F, Frossard JP. Increased pathogenicity of European porcine reproductive and respiratory syndrome virus is associated with enhanced adaptive responses and viral clearance. Vet Microbiol. 2013, 163: 13-22.<\/li>\n<li>Murtaugh MP, Elam MR, Kakach LT. Comparison of the structural protein coding sequences of the VR-2332 and Lelystad virus strains of the PRRS virus. Arch Virol. 1995, 140:1451-60.<\/li>\n<li>Murtaugh MP, Yuan S, Faaberg KS. Appearance of novel PRRSV isolates by recombination in the natural environment. Adv Exp Med Biol. 2001, 494:31-6.<\/li>\n<li>Murtaugh MP, Stadejek T, Abrahante JE, Lam TT, Leung FC. The ever-expanding diversity of porcine reproductive and respiratory syndrome virus. Virus Res. 2010, 154:18-30.<\/li>\n<li>Music N, Gagnon CA. The role of porcine reproductive and respiratory syndrome (PRRS) virus structural and non-structural proteins in virus pathogenesis. Anim Health Res Rev. 2010, 11:135-63.<\/li>\n<li>Oleksiewicz MB, Stadejek T, Ma\u0107kiewicz Z, Porowski M, Pejsak Z. Discriminating between serological responses to European-genotype live vaccine and European-genotype field strains of porcine reproductive and respiratory syndrome virus (PRRSV) by peptide ELISA. J Virol Methods. 2005, 129:134-44.<\/li>\n<li>Rowland RR, Steffen M, Ackerman T, Benfield DA. The evolution of porcine reproductive and respiratory syndrome virus: quasispecies and emergence of a virus subpopulation during infection of pigs with VR-2332. Virology. 1999, 259:262-6.<\/li>\n<li>Shi M, Lam TT, Hon CC, Hui RK, Faaberg KS, Wennblom T, Murtaugh MP, Stadejek T, Leung FC. Molecular epidemiology of PRRSV: a phylogenetic perspective. Virus Res. 2010, 154:7-17.<\/li>\n<li>Sinn LJ, Zieglowski L, Koinig H, Lamp B, Jansko B, M\u00f6\u00dflacher G, Riedel C, Hennig-Pauka I, R\u00fcmenapf T. Characterization of two Austrian porcine reproductive and respiratory syndrome virus (PRRSV) field isolates reveals relationship to East Asian strains. Vet Res.\u00a02016, \u00a047:17.<\/li>\n<li>Snijder EJ, Meulenberg JJ. The molecular biology of arteriviruses. J Gen Virol. 1998, 79:961-79. Snijder EJ, Dobbe JC, Spaan WJ. Heterodimerization of the two major proteins is essential for arterivirus infectivity. J Virol. 2003, 77:97-104. Snijder EJ, Kikkert M, Fang Y. Arterivirus molecular biology and pathogenesis. J Gen Virol. 2013, 94:2141-63.<\/li>\n<li>Spilman MS, Welbon C, Nelson E, Dokland T. Cryo-electron tomography of porcine reproductive and respiratory syndrome virus: organization of the nucleocapsid. J Gen Virol. 2009, 90:527-35.<\/li>\n<li>Stadejek T, Oleksiewicz MB, Potapchuk D, Podg\u00f3rska K. Porcine reproductive and respiratory syndrome virus strains of exceptional diversity in Eastern Europe support the definition of new genetic subtypes. J Gen Virol. 2006, 87:1835-41.<\/li>\n<li>Stadejek T, Stankevicius A, Murtaugh MP, Oleksiewicz MB. Molecular evolution of PRRSV in Europe: current state of play. Vet Microbiol. 2013, 165:21-8.<\/li>\n<li>Sun L, Li Y, Liu R, Wang X, Gao F, Lin T, Huang T, Yao H, Tong G, Fan H, Wei Z, Yuan S. Porcine reproductive and respiratory syndrome virus ORF5a protein is essential for virus viability. Virus Res. 2013, 171:178-85.<\/li>\n<li>Tian D, Wei Z, Zevenhoven-Dobbe JC, Liu R, Tong G, Snijder EJ, Yuan S. Arterivirus minor envelope proteins are a major determinant of viral tropism in cell culture. J Virol. 2012, 86:3701-12.<\/li>\n<li>Truong HM, Lu Z, Kutish GF, Galeota J, Osorio FA, Pattnaik AK. A highly pathogenic porcine reproductive and respiratory syndrome virus generated from an infectious cDNA clone retains the in vivo virulence and transmissibility properties of the parental virus. Virology. 2004, 325:308\u201319.<\/li>\n<li>Van Vugt JJ, Storgaard T, Oleksiewicz MB, B\u00f8tner A. High frequency RNA recombination in porcine reproductive and respiratory syndrome virus occurs preferentially between parental sequences with high similarity. J Gen Virol. 2001, 82:2615-20.<\/li>\n<li>Wang X, Marthaler D, Rovira A, Rossow S, Murtaugh MP. Emergence of a virulent porcine reproductive and respiratory syndrome virus in vaccinated herds in the United States. Virus Res. 2015, 210:34-41.<\/li>\n<li>Weiland E, Wieczorek-Krohmer M, Kohl D, Conzelmann KK, Weiland F. Monoclonal antibodies to the GP5 of porcine reproductive and respiratory syndrome virus are more effective in virus neutralization than monoclonal antibodies to the GP4. Vet Microbiol. 1999, 66:171-86.<\/li>\n<li>Wissink EH, Kroese MV, van Wijk HA, Rijsewijk FA, Meulenberg JJ, Rottier PJ. Envelope protein requirements for the assembly of infectious virions of porcine reproductive and respiratory syndrome virus. J Virol. 2005, 79:12495-506.<\/li>\n<li>Zhao K, Ye C, Chang XB, Jiang CG, Wang SJ, Cai XH, Tong GZ, Tian ZJ, Shi M, An TQ. Importation and Recombination Are Responsible for the Latest Emergence of Highly Pathogenic porcine reproductive and respiratory syndrome virus in China. J Virol. 2015, 89:10712-6.<\/li>\n<li>Zimmerman JJ, Benfield DA, Dee SA, Murtaugh MP, Stadejek T, Stevenson GW, Torremorell M. Porcine reproductive and respiratory syndrome virus (porcine arterivirus). In: 10th ed. Diseases of swine, Ed. Wiley-Blackwell. 2012, 31:463-86.<\/li>\n<\/ul>\n<\/p><\/div><\/div>[\/vc_column][\/vc_row]<\/p>\n<div style=\"text-align:center\" class=\"yasr-auto-insert-visitor\"><\/div><\/div>","protected":false},"excerpt":{"rendered":"<p>[vc_row][vc_column width=\u00bb1\/1&#8243;][vc_column_text el_class=\u00bbintro\u00bb]El genoma del virus del PRRS consiste en una sola cadena no segmentada de ARN de sentido\u00a0positivo. El ARN est\u00e1 compuesto por al menos diez fragmentos de lectura abierta (ORF por su\u00a0acr\u00f3nimo en ingl\u00e9s) y su tama\u00f1o total es de unas 15 kb.[\/vc_column_text][vc_column_text]Despu\u00e9s de la 5\u2019-UTR, en sentido de la traducci\u00f3n, se encuentran las ORFs 1a y 1b, las\u00a0cuales dan lugar a dos poliproteinas (pp1a y pp1b). Estas, tras su divisi\u00f3n, dan lugar a 14\u00a0prote\u00ednas no estructurales (nsp por su acr\u00f3nimo en ingl\u00e9s), incluyendo cuatro proteasas, la\u00a0ARN polimerasa ARN-dependiente, la helicasa y una endoribonucleasa. Estas prote\u00ednas se\u00a0expresan solo durante la replicaci\u00f3n y no forman parte del viri\u00f3n.[\/vc_column_text][vc_column_text] Continuando en el sentido de la traducci\u00f3n hasta llegar a 3\u2019 encontramos las ORFs de la 2 a la\u00a07 (ORF2a, ORF2b, ORF3, ORF4, ORF5, ORF5a, ORF6 y ORF7), que codifican para las prote\u00ednas\u00a0estructurales menores y mayores: Prote\u00ednas estructurales menores: tres N-glicosiladas: GP2a, GP3 y GP4, las\u00a0cuales forman un tr\u00edmero, y una no glicosilada: E o 2b. El complejo trim\u00e9rico,\u00a0solo o mediante la interacci\u00f3n con GP5, es esencial para la infectividad del\u00a0virus. La prote\u00edna E tambi\u00e9n interact\u00faa con el tr\u00edmero y es importante para la\u00a0replicaci\u00f3n y para el tropismo celular del virus. 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