200:, another protein layer, between the envelope and the genome. The virus wraps its delicate nucleic acid with a protein shell known as the capsid, from the Latin capsa, meaning "box," in order to shield it from this hostile environment. Similar to how numerous bricks come together to form a wall, the capsid is made up of one or more distinct protein types that repeatedly repeat to form the whole capsid. This repetitive pattern creates a robust but rather flexible capsid. The nucleic acid inside the capsid is appropriately protected by its modest size and physical difficulty in opening it. The nucleocapsid of the virion is made up of the nucleic acid and the capsid. Remember that the genomes of most viruses are very small. Genes code for instructions to make proteins, so small genomes cannot code for many proteins. Therefore, the virion capsid consists of one or only a few proteins that repeat over and over to form the structure. The viral nucleic acid would be physically too large to fit inside the capsid if it consisted of more than a few proteins. The capsid, having a focused role of protecting the genome in addition to immune recognition evasion. The viral capsid is known for its protection of RNA before it is inserted into the host cell, unlike the viral envelope which protects the protein capsid.
97:. One of the main parts of human pathogenic viruses is glycoprotein. They have been shown to play significant roles in immunity and infection. Viral glycoproteins, a new class of cellular inhibitory proteins has been discovered. These include the E3 ubiquitin ligases of the membrane-associated RING-CH (MARCH) family, which among other things, inhibits the expression of cell surface proteins implicated in adaptive immunity. Being made up mostly of host membrane, the viral envelope can also have the proteins associated with the host cell within their membrane after budding. Many enveloped viruses mature by budding at the plasma membrane, which allows them to be discharged from infected cells. During this procedure, viral transmembrane proteins, also known as
82:
triggering by the processes that go along with attachment and uptake, which frequently happens during transport of the fusion protein to the cell surface but may also happen extracellularly. So far, structural studies have revealed two kinds of viral fusion proteins. These proteins are believed to catalyze the same mechanism in both situations, resulting in the fusing of two bilayers. In other words, these proteins operate as enzymes, which while having various structural variations catalyze the same chemical reaction.
1301:
1549:
227:, therefore these viruses are easier to sterilize than non-enveloped viruses, have limited survival outside host environments, and typically must transfer directly from host to host. Viral envelope persistence, whether it be enveloped or naked, are a factor in determining longevity of a virus on inanimate surfaces. Enveloped viruses possess great adaptability and can change in a short time in order to evade the immune system. Enveloped viruses can cause
74:. Many enveloped viruses only have one protein visible on the surface of the particle, which is required for both mediating adhesion to the cell surface and for the subsequent membrane fusion process. To create potentially protective vaccines for human pathogenic enveloped viruses for which there is currently no vaccine, it is essential to comprehend how antibodies interact with viral envelope proteins, particularly with the fusion protein, and how
1537:
1573:
1561:
20:
189:
the fusion between the viral envelope and the host's cellular membrane. In some cases, the virus with an envelope will form an endosome within the host cell. There are three main types of viral glycoproteins: Envelope proteins, membrane proteins, and spike proteins (E, M, and S). The viral envelope then fuses with the host's membrane, allowing the capsid and viral
183:
and pseudo typed retroviruses have a harder time infecting TAM-deficient DCs, albeit infection can be brought back by type I IFN antibodies. A TAM kinase inhibitor, meanwhile, prevents infection of wild-type DCs. TAM receptors, which are potential targets for therapy, are thereby activated by viruses
125:
even in the absence of spike proteins by relying only on viral core components. The spike proteins can occasionally be produced as virus-like particles without the viral core. Therefore, optimal budding and release may be dependent on a coordinated "push-and-pull" action between core and spike, where
188:
on the host's membrane. The particular set of viral proteins are engaged in a series of structural changes. When these changes are set/finished, there is then and only then, fusion with the host membrane. These glycoproteins mediate the interaction between virion and host cell, typically initiating
66:
to fuse. Although there are effective vaccines against some of these viruses, there is no preventative or curative medicine for the majority of them. In most cases, the known vaccines operate by inducing antibodies that prevent the pathogen from entering cells. This happens in the case of enveloped
112:
For a very long time, it was thought that the spike proteins, which are necessary for infectivity, were directly incorporated into the viral core through their cytoplasmic domains. Recent research suggests that while such direct interactions may be what causes the budding of alphaviruses, this may
81:
Enveloped viruses enter cells by joining a cellular membrane to their lipid bilayer membrane. Priming by proteolytic processing, either of the fusion protein or of a companion protein, is necessary for the majority of viral fusion proteins. The priming stage then gets the fusion protein ready for
646:
Gelderblom HR. Structure and
Classification of Viruses. In: Baron S, editor. Medical Microbiology. 4th edition. Galveston (TX): University of Texas Medical Branch at Galveston; 1996. Chapter 41. Available from:
178:
signaling to circumvent host defenses and advance infection.TAM-deficient DCs exhibit type I IFN responses that are more pronounced than those of wild-type cells in response to viral exposure. As a result,
717:
Bhattacharyya, Suchita; ZagĂłrska, Anna; Lew, Erin D.; Shrestha, Bimmi; Rothlin, Carla V.; Naughton, John; Diamond, Michael S.; Lemke, Greg; Young, John A.T. (2013-08-14).
1866:
1861:
279:
1918:
441:
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2431:
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2421:
1054:
Firquet, Swan; Beaujard, Sophie; Lobert, Pierre-Emmanuel; Sané, Famara; Caloone, Delphine; Izard, Daniel; Hober, Didier (June 2015).
1897:
1892:
1887:
1611:
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171:
may be seen on the membranes of several enveloped viruses, which they employ to bind Gas6 and
Protein S to activate TAM receptors.
776:"New Biophysical Approaches Reveal the Dynamics and Mechanics of Type I Viral Fusion Machinery and Their Interplay with Membranes"
3149:
1225:
160:
2912:
39:. It protects the genetic material in their life cycle when traveling between host cells. Not all viruses have envelopes. A
1724:
2882:
2816:
2043:
914:
174:
Ligand-coated viruses stimulate type I IFN signaling, activate TAM receptors on dendritic cells (DCs), and suppress
2510:
2178:
1160:
102:
872:
Banerjee, Nilotpal, and Sumi
Mukhopadhyay. “Viral glycoproteins: biological role and application in diagnosis.”
234:
Vaccination against enveloped viruses can function by neutralizing the glycoprotein activity with antibodies.
3029:
1577:
719:"Enveloped Viruses Disable Innate Immune Responses in Dendritic Cells by Direct Activation of TAM Receptors"
2503:
2498:
1604:
184:
to reduce type I IFN signaling. Glycoproteins on the surface of the envelope serve to identify and bind to
3131:
3066:
2738:
2714:
2521:
2406:
2312:
2238:
2163:
2058:
1942:
1877:
1797:
1763:
1714:
1113:"Common Features of Enveloped Viruses and Implications for Immunogen Design for Next-Generation Vaccines"
470:"Common Features of Enveloped Viruses and Implications for Immunogen Design for Next-Generation Vaccines"
118:
1807:
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2018:
2001:
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447:
1597:
1254:
185:
3251:
3087:
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1812:
1460:
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Lun, Cheng Man; Waheed, Abdul A.; Majadly, Ahlam; Powell, Nicole; Freed, Eric O. (2021-03-16).
3221:
3112:
2992:
2864:
2724:
1211:
3023:
2961:
2648:
2092:
2083:
2005:
1952:
1773:
1664:
1512:
1507:
228:
8:
2694:
2088:
2078:
1997:
1502:
1487:
1249:
940:
Stuart, David I.; Ren, Jingshan; Wang, Xiangxi; Rao, Zihe; Fry, Elizabeth E. (May 2019).
149:
3216:
3093:
1137:
1112:
1088:
1055:
1031:
998:
974:
941:
925:
906:
894:
810:
775:
751:
718:
694:
661:
624:
591:
567:
534:
515:
502:
469:
175:
168:
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often dies or is weakened, and sheds more viral particles for an extended period. The
3283:
2668:
2416:
2355:
2120:
1536:
1477:
1322:
1142:
1093:
1075:
1036:
1018:
979:
961:
910:
841:
815:
797:
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738:
699:
681:
629:
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572:
554:
507:
489:
412:
153:
2930:
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2227:
1553:
1373:
1309:
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1124:
1083:
1067:
1026:
1010:
969:
953:
920:
902:
877:
857:
852:
White, Judith M, and Gary R Whittaker. “Fusion of
Enveloped Viruses in Endosomes.”
837:
805:
787:
746:
730:
689:
673:
619:
603:
592:"Mechanism of Viral Glycoprotein Targeting by Membrane-Associated RING-CH Proteins"
562:
546:
519:
497:
481:
1589:
3160:
2617:
2607:
2360:
1383:
1368:
1363:
1347:
304:
24:
957:
3234:
3117:
1988:
1908:
1541:
1472:
1440:
1327:
1189:
1128:
734:
485:
359:
299:
259:
130:
71:
59:
1014:
881:
648:
550:
70:
The membrane fusion event that triggers viral entrance is caused by the viral
3277:
3183:
2834:
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1932:
1649:
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1404:
1337:
1290:
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1022:
965:
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417:
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364:
249:
208:
133:
98:
90:
86:
63:
666:
BioEssays: News and
Reviews in Molecular, Cellular and Developmental Biology
2903:
2855:
2807:
2759:
2680:
2465:
2301:
1978:
1787:
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1414:
1399:
1378:
1300:
1234:
1146:
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819:
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633:
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511:
381:
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349:
329:
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264:
180:
141:
114:
94:
1071:
703:
607:
204:
122:
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2786:
2106:
2069:
1445:
1424:
1342:
1317:
396:
309:
294:
289:
284:
212:
1164:
832:
Navaratnarajah, C.K. et al. “Assembly of
Viruses: Enveloped Particles.”
3125:
3057:
2654:
2460:
2291:
2287:
1522:
1497:
1056:"Survival of Enveloped and Non-Enveloped Viruses on Inanimate Surfaces"
391:
386:
314:
254:
224:
216:
106:
75:
62:, and they infect their target cells by causing the viral envelope and
1203:
861:
792:
3171:
3166:
3107:
3101:
2345:
2222:
2212:
2200:
1973:
1637:
1482:
1419:
1409:
1332:
319:
164:
145:
1753:
1264:
535:"Viral glycoproteins: biological role and application in diagnosis"
1153:
67:
viruses when the antibodies bind to the viral envelope proteins.
48:
716:
58:
Numerous human pathogenic viruses in circulation are encased in
3013:
2951:
2699:
2638:
2531:
2029:
1685:
1517:
1280:
197:
190:
157:
52:
342:
The following are some examples of viruses without envelopes:
85:
The envelopes are typically derived from portions of the host
2584:
2574:
2569:
2559:
2554:
2549:
2544:
2151:
2146:
2141:
1238:
36:
242:
The following are some examples of enveloped virus species:
19:
3136:
2967:
2579:
2564:
1993:
1729:
220:
660:
Cadd, T. L.; Skoging, U.; Liljeström, P. (November 1997).
3197:
3193:
3176:
2322:
2173:
1053:
148:
cells and inhibit immunological responses brought on by
662:"Budding of enveloped viruses from the plasma membrane"
589:
443:
659:
533:
Banerjee, Nilotpal; Mukhopadhyay, Sumi (March 2016).
211:
envelope of these viruses is relatively sensitive to
16:
Outermost layer of many types of the infectious agent
532:
337:
1619:
1192:. Molecular Expressions: Images from the Microscope
126:oligomerization of both components is essential.
3275:
939:
237:
774:Benhaim, Mark A.; Lee, Kelly K. (2020-04-08).
51:in the envelope, which may be acquired by the
3233:
1605:
1219:
1111:Rey, Felix A.; Lok, Shee-Mei (8 March 2018).
2902:
2854:
2806:
2758:
435:
433:
3242:
2068:
999:"Capsid and Infectivity in Virus Detection"
946:Cold Spring Harbor Perspectives in Medicine
649:https://www.ncbi.nlm.nih.gov/books/NBK8174/
468:Rey, Felix A.; Lok, Shee-Mei (2018-03-08).
1612:
1598:
1226:
1212:
773:
2769:Parainfluenza hemagglutinin-neuraminidase
1136:
1087:
1030:
973:
924:
809:
791:
750:
693:
623:
566:
501:
430:
1468:Laboratory diagnosis of viral infections
35:is the outermost layer of many types of
18:
1233:
3276:
3012:
2950:
2028:
1684:
1110:
996:
892:
467:
156:(IFNs) when they are activated by the
93:and proteins), but include some viral
2913:Respiratory syncytial virus G protein
1593:
1207:
3000:
2938:
2890:
2842:
2794:
2746:
2310:
2236:
1940:
1795:
1761:
1560:
942:"Hepatitis A Virus Capsid Structure"
895:"Virus Structure and Classification"
439:
1572:
13:
907:10.1016/B978-0-12-800947-5.00002-8
196:All enveloped viruses also have a
14:
3295:
2817:Mumps hemagglutinin-neuraminidase
1182:
338:Examples of non-enveloped viruses
2179:Hepatitis B virus DNA polymerase
1571:
1559:
1548:
1547:
1535:
1299:
842:10.1016/B978-012374410-4.00667-1
129:They may help viruses avoid the
2010:(non-enveloped circular ds-DNA)
1104:
1047:
1003:Food and Environmental Virology
990:
933:
886:
866:
846:
101:, are integrated into membrane
826:
767:
710:
653:
640:
583:
526:
461:
193:to enter and infect the host.
1:
3030:Vesiculovirus matrix proteins
423:
238:Examples of enveloped viruses
105:containing components of the
203:The cell from which a virus
55:from an infected host cell.
7:
3067:Structure and genome of HIV
2124:(circular partially ds-DNA)
958:10.1101/cshperspect.a031807
856:vol. 17,6 (2016): 593-614.
406:
119:negative strand RNA viruses
10:
3300:
1700:Herpesvirus glycoprotein B
1129:10.1016/j.cell.2018.02.054
735:10.1016/j.chom.2013.07.005
486:10.1016/j.cell.2018.02.054
3210:
3147:
3074:
3065:
3056:
2991:
2929:
2881:
2833:
2785:
2737:
2712:
2679:
2637:
2625:
2616:
2601:
2519:
2474:
2459:
2404:
2369:
2354:
2339:
2286:
2221:
2208:
2199:
2161:
2130:
2119:
2056:
2016:
1987:
1969:
1931:
1906:
1875:
1849:
1840:
1829:
1786:
1752:
1712:
1695:HHV capsid portal protein
1672:
1663:
1645:
1636:
1531:
1433:
1392:
1356:
1308:
1297:
1273:
1260:Social history of viruses
1245:
1060:Microbes and Environments
1015:10.1007/s12560-009-9020-y
893:Louten, Jennifer (2016).
882:10.1007/s13337-015-0293-5
551:10.1007/s13337-015-0293-5
138:receptor tyrosine kinases
121:. These viruses can form
997:Cliver, Dean O. (2009).
899:Essential Human Virology
876:vol. 27,1 (2016): 1-11.
834:Encyclopedia of Virology
2690:Influenza hemagglutinin
723:Cell Host & Microbe
3252:Gag-onc fusion protein
1461:Helper dependent virus
678:10.1002/bies.950191109
41:viral envelope protein
28:
3222:murine leukemia virus
3113:Reverse transcriptase
2993:Indiana vesiculovirus
2865:Measles hemagglutinin
1163:. CDC. Archived from
1072:10.1264/jsme2.ME14145
608:10.1128/mBio.00219-21
229:persistent infections
22:
1953:Early 35 kDa protein
1513:Virus quantification
1508:Virus classification
440:HURLBERT, RONALD E.
113:not be the case for
78:neutralize viruses.
1503:Virus-like particle
167:. The phospholipid
150:Toll-like receptors
3217:Rous sarcoma virus
1161:"The Rabies Virus"
176:type II interferon
169:phosphatidylserine
154:type I interferons
29:
3271:
3270:
3267:
3266:
3263:
3262:
3259:
3258:
3206:
3205:
3052:
3051:
3048:
3047:
3044:
3043:
3040:
3039:
2987:
2986:
2983:
2982:
2925:
2924:
2921:
2920:
2877:
2876:
2873:
2872:
2829:
2828:
2825:
2824:
2781:
2780:
2777:
2776:
2733:
2732:
2708:
2707:
2597:
2596:
2593:
2592:
2455:
2454:
2335:
2334:
2331:
2330:
2282:
2281:
2195:
2194:
2191:
2190:
2187:
2186:
2115:
2114:
2102:
2101:
2052:
2051:
1965:
1964:
1961:
1960:
1927:
1926:
1825:
1824:
1821:
1820:
1782:
1781:
1748:
1747:
1708:
1707:
1587:
1586:
1478:Neurotropic virus
1323:Viral replication
1190:"Virus Structure"
862:10.1111/tra.12389
836:(2008): 193–200.
793:10.3390/v12040413
413:Bacterial capsule
27:, coat = envelope
3291:
3240:
3239:
3231:
3230:
3072:
3071:
3063:
3062:
3010:
3009:
2998:
2997:
2948:
2947:
2936:
2935:
2931:Zaire ebolavirus
2900:
2899:
2888:
2887:
2852:
2851:
2840:
2839:
2804:
2803:
2792:
2791:
2756:
2755:
2744:
2743:
2635:
2634:
2623:
2622:
2614:
2613:
2537:3C-like protease
2472:
2471:
2367:
2366:
2352:
2351:
2308:
2307:
2234:
2233:
2228:Duplornaviricota
2219:
2218:
2206:
2205:
2128:
2127:
2066:
2065:
2026:
2025:
2014:
2013:
1985:
1984:
1938:
1937:
1847:
1846:
1838:
1837:
1793:
1792:
1759:
1758:
1682:
1681:
1670:
1669:
1661:
1660:
1643:
1642:
1614:
1607:
1600:
1591:
1590:
1575:
1574:
1563:
1562:
1551:
1550:
1539:
1374:Phenotype mixing
1310:Viral life cycle
1303:
1228:
1221:
1214:
1205:
1204:
1200:
1198:
1197:
1176:
1175:
1173:
1172:
1157:
1151:
1150:
1140:
1123:(6): 1319–1334.
1108:
1102:
1101:
1091:
1051:
1045:
1044:
1034:
994:
988:
987:
977:
937:
931:
930:
928:
890:
884:
870:
864:
850:
844:
830:
824:
823:
813:
795:
771:
765:
764:
754:
714:
708:
707:
697:
672:(11): 993–1000.
657:
651:
644:
638:
637:
627:
602:(2): e00219–21.
587:
581:
580:
570:
530:
524:
523:
505:
480:(6): 1319–1334.
465:
459:
458:
456:
455:
446:. Archived from
437:
300:Orthomyxoviruses
3299:
3298:
3294:
3293:
3292:
3290:
3289:
3288:
3274:
3273:
3272:
3255:
3202:
3161:transactivators
3143:
3036:
2979:
2917:
2869:
2821:
2773:
2729:
2704:
2675:
2618:Influenza virus
2608:Negarnaviricota
2605:
2603:
2589:
2515:
2463:
2451:
2400:
2361:Kitrinoviricota
2358:
2343:
2341:
2327:
2299:
2278:
2225:
2210:
2183:
2157:
2123:
2111:
2098:
2048:
2009:
1991:
1977:
1971:
1957:
1923:
1902:
1871:
1833:
1832:(Duplodnaviria,
1831:
1830:circular ds-DNA
1817:
1778:
1744:
1704:
1653:
1647:
1632:
1618:
1588:
1583:
1527:
1429:
1388:
1384:Viral evolution
1369:Antigenic shift
1364:Antigenic drift
1352:
1348:Lysogenic cycle
1304:
1295:
1269:
1241:
1232:
1195:
1193:
1188:
1185:
1180:
1179:
1170:
1168:
1159:
1158:
1154:
1109:
1105:
1052:
1048:
995:
991:
938:
934:
917:
891:
887:
871:
867:
851:
847:
831:
827:
772:
768:
715:
711:
658:
654:
645:
641:
588:
584:
531:
527:
466:
462:
453:
451:
438:
431:
426:
409:
340:
305:Paramyxoviridae
240:
25:Cytomegalovirus
23:Schematic of a
17:
12:
11:
5:
3297:
3287:
3286:
3269:
3268:
3265:
3264:
3261:
3260:
3257:
3256:
3254:
3249:
3247:
3237:
3235:Fusion protein
3228:
3227:
3226:
3225:
3224:
3219:
3208:
3207:
3204:
3203:
3201:
3200:
3191:
3186:
3181:
3180:
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3156:
3154:
3145:
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3141:
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3134:
3122:
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3120:
3118:HIV-1 protease
3115:
3110:
3098:
3097:
3096:
3083:
3081:
3069:
3060:
3054:
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3024:matrix protein
3019:
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3007:
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2989:
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2962:matrix protein
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2697:
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2677:
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2663:viral envelope
2659:
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2649:matrix protein
2644:
2642:
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2620:
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2604:negative-sense
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2011:
1989:Polyomaviridae
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1834:Varidnaviria?)
1827:
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1658:
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1183:External links
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952:(5): a031807.
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99:spike proteins
87:cell membranes
72:fusion protein
60:lipid bilayers
33:viral envelope
15:
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1650:Duplodnaviria
1646:linear ds-DNA
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1493:Viral disease
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1405:Bacteriophage
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1355:
1349:
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1341:
1339:
1338:Virus latency
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1326:
1324:
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1315:
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1292:
1291:Viral protein
1289:
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1279:
1278:
1276:
1272:
1266:
1263:
1261:
1258:
1256:
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1229:
1224:
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1210:
1209:
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1191:
1187:
1186:
1167:on 2017-01-18
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450:on 2008-11-10
449:
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418:Cell envelope
416:
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377:Caliciviruses
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365:Anelloviruses
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326:Retroviruses
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251:
250:Herpesviridae
248:
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235:
232:
230:
226:
222:
218:
214:
210:
209:lipid bilayer
206:
201:
199:
194:
192:
187:
182:
177:
172:
170:
166:
162:
159:
155:
151:
147:
144:clearance of
143:
139:
135:
134:immune system
132:
127:
124:
123:bud particles
120:
116:
110:
108:
104:
100:
96:
95:glycoproteins
92:
91:phospholipids
88:
83:
79:
77:
73:
68:
65:
64:cell membrane
61:
56:
54:
50:
46:
42:
38:
34:
26:
21:
3159:
3148:
3124:
3100:
3086:
3075:
3022:
3001:
2960:
2939:
2904:glycoprotein
2891:
2856:glycoprotein
2843:
2808:glycoprotein
2795:
2760:glycoprotein
2747:
2713:
2681:glycoprotein
2662:
2661:
2647:
2626:
2520:
2511:Nucleocapsid
2487:
2486:
2475:
2466:Pisuviricota
2405:
2382:
2381:
2370:
2311:
2302:Pisuviricota
2237:
2162:
2131:
2057:
2017:
1979:Monodnaviria
1941:
1907:
1876:
1850:
1842:Epstein–Barr
1796:
1788:Adenoviridae
1762:
1713:
1673:
1655:Varidnaviria
1576:
1564:
1552:
1540:
1456:Viral vector
1451:Helper virus
1415:Human virome
1400:Animal virus
1379:Reassortment
1285:
1255:Introduction
1235:Microbiology
1194:. Retrieved
1169:. Retrieved
1165:the original
1155:
1120:
1116:
1106:
1063:
1059:
1049:
1006:
1002:
992:
949:
945:
935:
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874:Virusdisease
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769:
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669:
665:
655:
642:
599:
595:
585:
542:
539:Virusdisease
538:
528:
477:
473:
463:
452:. Retrieved
448:the original
442:
392:Astroviruses
373:RNA viruses
355:Parvoviruses
350:Adenoviruses
346:DNA viruses
341:
330:Retroviruses
315:Bunyaviruses
280:Alphaviridae
275:Flaviviridae
271:RNA viruses
265:Asfarviridae
246:DNA viruses
241:
233:
215:, heat, and
202:
195:
181:flaviviruses
173:
128:
115:retroviruses
111:
84:
80:
69:
57:
44:
40:
32:
30:
3244:oncoprotein
2356:Hepatitis C
2121:Hepatitis B
2107:Agnoprotein
2070:oncoprotein
2044:VP2 and VP3
1578:WikiProject
1446:Giant virus
1425:Plant virus
1343:Lytic cycle
1318:Viral entry
786:(4): E413.
545:(1): 1–11.
397:Hepeviridae
320:Filoviruses
310:Rhabdovirus
295:Hepatitis D
290:Coronavirus
285:Togaviridae
217:amphiphiles
213:desiccation
109:(capsid).
2669:M2 protein
2655:M1 protein
2461:SARS-CoV-2
1523:Virosphere
1498:Viral load
1488:Satellites
1274:Components
1196:2007-06-27
1171:2008-11-07
454:2008-11-07
424:References
387:Reoviruses
255:Poxviridae
225:detergents
142:phagocytic
107:viral core
76:antibodies
3211:Multiple
3108:Integrase
2346:Riboviria
2223:Rotavirus
2213:Riboviria
1974:Riboviria
1483:Oncovirus
1420:Mycovirus
1410:Virophage
1333:Viroplasm
1080:1342-6311
1023:1867-0334
966:2157-1422
901:: 19–29.
802:1999-4915
743:1931-3128
686:0265-9247
616:2150-7511
559:2347-3584
494:0092-8674
165:Protein S
146:apoptotic
140:increase
45:E protein
3284:Virology
3278:Category
2504:Membrane
2499:Envelope
2093:SV40 Tag
1754:Vaccinia
1554:Category
1357:Genetics
1265:Virology
1147:29522750
1098:25843687
1041:20234879
984:30037986
820:32276357
761:23954153
634:33727347
577:26925438
512:29522750
407:See also
219:such as
103:vesicles
2835:Measles
2288:Rhinov.
1735:ICP34.5
1566:Commons
1393:By host
1250:History
1138:7112304
1089:4462923
1032:2837222
975:6496327
926:7150055
854:Traffic
811:7232462
780:Viruses
752:3779433
704:9394621
695:7161837
625:8092221
568:4758313
520:3775608
503:7112304
158:ligands
49:protein
37:viruses
3014:capsid
2952:capsid
2700:HA-tag
2639:capsid
2602:ss-RNA
2532:ORF1ab
2340:ss-RNA
2300:etc. (
2209:ds-RNA
2030:capsid
1898:EBNA-3
1893:EBNA-2
1888:EBNA-1
1686:capsid
1542:Portal
1518:Virome
1281:Capsid
1145:
1135:
1096:
1086:
1078:
1039:
1029:
1021:
982:
972:
964:
923:
913:
818:
808:
800:
759:
749:
741:
702:
692:
684:
632:
622:
614:
575:
565:
557:
518:
510:
500:
492:
198:capsid
191:genome
136:. TAM
53:capsid
3150:VRAPs
3132:gp120
2787:Mumps
2585:ORF9b
2575:ORF7b
2570:ORF7a
2560:ORF3d
2555:ORF3c
2550:ORF3b
2545:ORF3a
2539:(NS5)
2494:Spike
2296:Hep A
2292:Polio
2152:HBeAg
2147:HBcAg
2142:HBsAg
2006:HaPyV
2002:MCPyV
1970:other
1909:ncRNA
1867:LMP-2
1862:LMP-1
1740:ICP47
1725:vmw65
1625:early
1434:Other
1239:Virus
516:S2CID
47:is a
3137:gp41
3077:VSPs
3003:VSPs
2973:VP24
2968:VP40
2941:VSPs
2893:VSPs
2845:VSPs
2797:VSPs
2749:VSPs
2715:VNPs
2628:VSPs
2580:ORF8
2565:ORF6
2522:VNPs
2477:VSPs
2447:NS5B
2442:NS5A
2437:NS4B
2432:NS4A
2407:VNPs
2372:VSPs
2313:VNPs
2274:NSP6
2269:NSP5
2264:NSP4
2259:NSP3
2254:NSP2
2249:NSP1
2239:VNPs
2164:VNPs
2133:VSPs
2089:LTag
2084:MTag
2079:STag
2059:VNPs
2019:VSPs
1998:MPyV
1994:SV40
1943:VNPs
1919:EBER
1878:VNPs
1852:VSPs
1798:VNPs
1774:B13R
1764:VNPs
1730:ICP8
1715:VNPs
1675:VSPs
1629:late
1627:and
1143:PMID
1117:Cell
1094:PMID
1076:ISSN
1037:PMID
1019:ISSN
980:PMID
962:ISSN
911:ISBN
816:PMID
798:ISSN
757:PMID
739:ISSN
700:PMID
682:ISSN
630:PMID
612:ISSN
596:mBio
573:PMID
555:ISSN
508:PMID
490:ISSN
474:Cell
223:and
221:soap
205:buds
163:and
161:Gas6
152:and
131:host
117:and
3198:Vpx
3196:or
3194:Vpu
3189:Vif
3184:Nef
3177:Vpr
3172:Rev
3167:Tat
3126:env
3102:pol
3094:p24
3088:gag
2883:RSV
2725:NS1
2427:NS3
2422:NS2
2323:VPg
2201:RNA
2174:HBx
2039:VP1
1813:E1B
1808:E1A
1638:DNA
1133:PMC
1125:doi
1121:172
1084:PMC
1068:doi
1027:PMC
1011:doi
970:PMC
954:doi
921:PMC
903:doi
878:doi
858:doi
838:doi
806:PMC
788:doi
747:PMC
731:doi
690:PMC
674:doi
620:PMC
604:doi
563:PMC
547:doi
498:PMC
482:doi
478:172
43:or
3280::
3058:RT
2417:P7
2394:E2
2389:E1
2294:,
2290:,
2004:,
2000:,
1996:,
1237::
1141:.
1131:.
1119:.
1115:.
1092:.
1082:.
1074:.
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1062:.
1058:.
1035:.
1025:.
1017:.
1005:.
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960:.
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668:.
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610:.
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594:.
571:.
561:.
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514:.
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488:.
476:.
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231:.
31:A
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3079::
3016::
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2363:)
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2061::
2032::
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1992:(
1981:)
1976:,
1972:(
1945::
1911::
1880::
1854::
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1100:.
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956::
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929:.
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822:.
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