{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,10]],"date-time":"2026-03-10T16:34:33Z","timestamp":1773160473927,"version":"3.50.1"},"reference-count":60,"publisher":"American Society for Microbiology","issue":"8","license":[{"start":{"date-parts":[[1998,8,1]],"date-time":"1998-08-01T00:00:00Z","timestamp":901929600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[1998,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The GP\n            <jats:sub>3<\/jats:sub>\n            protein of the IAF-Klop strain of porcine reproductive and respiratory syndrome virus (PRRSV) was expressed in 293 cells by a recombinant human type 5 adenovirus carrying the open reading frame 3 gene. The protein exhibited a molecular mass of 42 kDa and comigrated with GP\n            <jats:sub>3<\/jats:sub>\n            expressed in PRRSV-infected MARC-145 cells. Removal of N-linked glycans from GP\n            <jats:sub>3<\/jats:sub>\n            resulted in a 27-kDa protein (P3), confirming its highly glycosylated nature. Pulse-chase experiments carried out either in the context of PRRSV infection or upon individual expression of GP\n            <jats:sub>3<\/jats:sub>\n            in 293 cells showed that the protein remains completely endo-\u03b2-\n            <jats:italic>N<\/jats:italic>\n            -acetylglucosaminidase H-sensitive even after 4 h of synthesis. Thus, the transport of GP\n            <jats:sub>3<\/jats:sub>\n            was restricted to the premedial Golgi compartment, presumably the endoplasmic reticulum (ER). However, a minor fraction of GP\n            <jats:sub>3<\/jats:sub>\n            was found to be secreted in the culture medium as a soluble membrane-free form. This released protein (sGP\n            <jats:sub>3<\/jats:sub>\n            ) was readily identified upon individual expression of GP\n            <jats:sub>3<\/jats:sub>\n            in 293 cells as well as in the context of PRRSV infection, albeit at lower levels. The sGP\n            <jats:sub>3<\/jats:sub>\n            migrated as a smear and displayed a molecular mass ranging from 43 to 53 kDa. The unglycosylated form of sGP\n            <jats:sub>3<\/jats:sub>\n            comigrated with its intracellular deglycosylated counterpart, suggesting that the release from the cell of a subset of GP\n            <jats:sub>3<\/jats:sub>\n            did not result from cleavage of a putative membrane-anchor sequence. Strikingly, unlike GP\n            <jats:sub>3<\/jats:sub>\n            , the sGP\n            <jats:sub>3<\/jats:sub>\n            acquired Golgi-specific modifications of its carbohydrate side chains and folded into a disulfide-linked homodimer. Brefeldin A treatment completely abolished the release of sGP\n            <jats:sub>3<\/jats:sub>\n            , suggesting that the ER-to-Golgi compartment is an obligatory step in cellular secretion of sGP\n            <jats:sub>3<\/jats:sub>\n            . In contrast, 10 mM monensin did not prevent sGP\n            <jats:sub>3<\/jats:sub>\n            release but inhibited the terminal glycosylation that confers on the protein its diffuse pattern. Since GP\n            <jats:sub>3<\/jats:sub>\n            was found to be nonstructural in the case of the North American strain, secretion of a minor fraction of GP\n            <jats:sub>3<\/jats:sub>\n            might be an explanation for its high degree of immunogenicity in infected pigs. Furthermore, this secreted protein might be relevant as a model for further studies on the cellular subcompartments involved in the sorting of proteins to the extracellular milieu.\n          <\/jats:p>","DOI":"10.1128\/jvi.72.8.6298-6306.1998","type":"journal-article","created":{"date-parts":[[2019,12,31]],"date-time":"2019-12-31T18:16:08Z","timestamp":1577816168000},"page":"6298-6306","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":46,"title":["A Subset of Porcine Reproductive and Respiratory Syndrome Virus GP\n            <sub>3<\/sub>\n            Glycoprotein Is Released into the Culture Medium of Cells as a Non-Virion-Associated and Membrane-Free (Soluble) Form"],"prefix":"10.1128","volume":"72","author":[{"given":"Helmi","family":"Mardassi","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Centre de Recherche en Virologie, Institut Armand-Frappier, Universite\u0301 du Que\u0301bec, Laval, Que\u0301bec, Canada H7N 4Z3,1 and"},{"name":"<!--label omitted: 2-->Institut de Recherche en Biotechnologie, Montre\u0301al, Que\u0301bec, Canada H4P 2R22"}]},{"given":"Patrick","family":"Gonin","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Centre de Recherche en Virologie, Institut Armand-Frappier, Universite\u0301 du Que\u0301bec, Laval, Que\u0301bec, Canada H7N 4Z3,1 and"}]},{"given":"Carl A.","family":"Gagnon","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Centre de Recherche en Virologie, Institut Armand-Frappier, Universite\u0301 du Que\u0301bec, Laval, Que\u0301bec, Canada H7N 4Z3,1 and"},{"name":"<!--label omitted: 2-->Institut de Recherche en Biotechnologie, Montre\u0301al, Que\u0301bec, Canada H4P 2R22"}]},{"given":"Bernard","family":"Massie","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Institut de Recherche en Biotechnologie, Montre\u0301al, Que\u0301bec, Canada H4P 2R22"}]},{"given":"Serge","family":"Dea","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Centre de Recherche en Virologie, Institut Armand-Frappier, Universite\u0301 du Que\u0301bec, Laval, Que\u0301bec, Canada H7N 4Z3,1 and"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","first-page":"578","article-title":"A differential efficiency of adenovirus-mediated in vivo gene transfer into skeletal muscle cells of different maturity","volume":"3","author":"Ascadi G.","year":"1994","unstructured":"Ascadi G. Jani A. Massie B. Simoneau M. Holland P. Blaschuk K. Karpati G. A differential efficiency of adenovirus-mediated in vivo gene transfer into skeletal muscle cells of different maturity.Hum. Mol. Genet. 3 1994 578 584","journal-title":"Hum. Mol. Genet."},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.102.5.1558"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1991.tb07827.x"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.88.3.1059"},{"key":"e_1_3_2_6_2","first-page":"629","article-title":"Nidovirales: a new order comprising Coronaviridae and Arteriviridae","volume":"142","author":"Cavanagh D.","year":"1997","unstructured":"Cavanagh D. Nidovirales: a new order comprising Coronaviridae and Arteriviridae.Arch. Virol. 142 1997 629 633","journal-title":"Arch. Virol."},{"key":"e_1_3_2_7_2","unstructured":"Chambers\nJ. J. A.\nRickwood\nD.\nFractionation of subcellular organelles by differential centrifugation\nCentrifugation: a practical approach.\nRickwood\nD.\n1978\n33\n47\nInformation Retrieval Ltd.\nWashington D.C"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.65.3.1427-1439.1991"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1993.1129"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(88)90381-9"},{"key":"e_1_3_2_11_2","first-page":"801","article-title":"Swine reproductive and respiratory syndrome in Quebec: isolation of an enveloped virus serologically-related to Lelystad virus","volume":"33","author":"Dea S.","year":"1992","unstructured":"Dea S. Bilodeau R. Athanassious R. Sauvageau R. Martineau G. P. Swine reproductive and respiratory syndrome in Quebec: isolation of an enveloped virus serologically-related to Lelystad virus.Can. Vet. J. 33 1992 801 808","journal-title":"Can. Vet. J."},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.65.6.2910-2920.1991"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.66.11.6294-6303.1992"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.69.6.3441-3448.1995"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1006\/smvy.1997.0104"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.63.6.2452-2456.1989"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1993.1164"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0378-1135(96)01328-4"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1995.1509"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1996.8310"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(95)90026-8"},{"key":"e_1_3_2_22_2","unstructured":"Gonin\nP.\nGagnon\nC. A.\nMassie\nB.\nDea\nS.\nProcaryotic and eucaryotic expression of ORFs 2 to 4 of porcine reproductive and respiratory syndrome virus abstr. VM5\nAbstracts of the 47th Annual Meeting of the Canadian Society of Microbiologists 1997.\n1997\n86\nCanadian Society of Microbiologists\nOttawa Ontario Canada"},{"key":"e_1_3_2_23_2","unstructured":"Gonin P. H. Mardassi C. A. Gagnon B. Massie and S. Dea. The ORF3 gene of the Quebec IAF-Klop strain of porcine reproductive and respiratory syndrome virus encodes a nonstructural and antigenic glycoprotein. Arch. Virol. in press."},{"key":"e_1_3_2_24_2","unstructured":"Gonin P. B. Pirzadeh C. A. Gagnon and S. Dea. Seroneutralization of porcine reproductive and respiratory syndrome virus correlates with antibody response to the GP 5 major envelope glycoprotein. J. Vet. Diagn. Invest. in press."},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.1099\/0022-1317-36-1-59"},{"key":"e_1_3_2_26_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.65.3.1177-1186.1991"},{"key":"e_1_3_2_27_2","first-page":"801","article-title":"Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum","volume":"56","author":"Jackson M. R.","year":"1990","unstructured":"Jackson M. R. Nilsson T. Peterson P. A. Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum.Cell 56 1990 801 813","journal-title":"Cell"},{"key":"e_1_3_2_28_2","doi-asserted-by":"publisher","DOI":"10.1016\/0378-1135(94)00113-B"},{"key":"e_1_3_2_29_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF01313785"},{"key":"e_1_3_2_30_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.116.5.1071"},{"key":"e_1_3_2_31_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(87)90418-9"},{"key":"e_1_3_2_32_2","doi-asserted-by":"publisher","DOI":"10.1038\/332462a0"},{"key":"e_1_3_2_33_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.70.3.1570-1579.1996"},{"key":"e_1_3_2_34_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(89)90685-5"},{"key":"e_1_3_2_35_2","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1995.tb07220.x"},{"key":"e_1_3_2_36_2","doi-asserted-by":"publisher","DOI":"10.1099\/0022-1317-75-12-3603"},{"key":"e_1_3_2_37_2","first-page":"55","article-title":"Porcine reproductive and respiratory syndrome virus: morphological, biochemical and serological characteristics of Quebec isolates associated to acute and chronic outbreaks of PRRS","volume":"58","author":"Mardassi H.","year":"1994","unstructured":"Mardassi H. Athanassious R. Mounir S. Dea S. Porcine reproductive and respiratory syndrome virus: morphological, biochemical and serological characteristics of Quebec isolates associated to acute and chronic outbreaks of PRRS.Can. J. Vet. Res. 58 1994 55 64","journal-title":"Can. J. Vet. Res."},{"key":"e_1_3_2_38_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1996.0356"},{"key":"e_1_3_2_39_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF01322667"},{"key":"e_1_3_2_40_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.72.3.2289-2296.1998"},{"key":"e_1_3_2_41_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1996.0573"},{"key":"e_1_3_2_42_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1993.1008"},{"key":"e_1_3_2_43_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0042-6822(95)80030-1"},{"key":"e_1_3_2_44_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.71.8.6061-6067.1997"},{"key":"e_1_3_2_45_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.118.2.267"},{"key":"e_1_3_2_46_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(87)90086-9"},{"key":"e_1_3_2_47_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(82)91500-5"},{"key":"e_1_3_2_48_2","doi-asserted-by":"publisher","DOI":"10.1038\/364771a0"},{"key":"e_1_3_2_49_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(82)90430-2"},{"key":"e_1_3_2_50_2","doi-asserted-by":"publisher","DOI":"10.1023\/A:1007931322271"},{"key":"e_1_3_2_51_2","first-page":"29","article-title":"Morphogenesis of Lelystad virus in porcine lung alveolar macrophages","volume":"4","author":"Pol J.","year":"1992","unstructured":"Pol J. Wagenaar F. Morphogenesis of Lelystad virus in porcine lung alveolar macrophages.Am. Assoc. Swine Pract. Newsl. 4 1992 29","journal-title":"Am. Assoc. Swine Pract. Newsl."},{"key":"e_1_3_2_52_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.66.5.2792-2797.1992"},{"key":"e_1_3_2_53_2","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1994.tb06434.x"},{"key":"e_1_3_2_54_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(83)90286-6"},{"key":"e_1_3_2_55_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.70.7.4767-4772.1996"},{"key":"e_1_3_2_56_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0968-0004(97)01122-5"},{"key":"e_1_3_2_57_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.64.1.339-346.1990"},{"key":"e_1_3_2_58_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.2842866"},{"key":"e_1_3_2_59_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/14.11.4683"},{"key":"e_1_3_2_60_2","doi-asserted-by":"publisher","DOI":"10.1099\/0022-1317-74-10-2061"},{"key":"e_1_3_2_61_2","doi-asserted-by":"publisher","DOI":"10.1016\/0378-1135(96)00047-8"}],"container-title":["Journal of Virology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/JVI.72.8.6298-6306.1998","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/JVI.72.8.6298-6306.1998","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,3,5]],"date-time":"2022-03-05T03:02:47Z","timestamp":1646449367000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/JVI.72.8.6298-6306.1998"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,8]]},"references-count":60,"journal-issue":{"issue":"8","published-print":{"date-parts":[[1998,8]]}},"alternative-id":["10.1128\/JVI.72.8.6298-6306.1998"],"URL":"https:\/\/doi.org\/10.1128\/jvi.72.8.6298-6306.1998","relation":{},"ISSN":["0022-538X","1098-5514"],"issn-type":[{"value":"0022-538X","type":"print"},{"value":"1098-5514","type":"electronic"}],"subject":[],"published":{"date-parts":[[1998,8]]},"assertion":[{"value":"1998-01-28","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"1998-04-21","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"1998-08-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}