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4_1_Orthomyxovirus1

4_1_Orthomyxovirus1 - Samuel E MCDB 134 C TABLE 2...

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Unformatted text preview: Samuel E. MCDB 134 C. TABLE 2. Influenza A virus genome RNA segments and coding assignments Orthomyxoviridae (influenza virus) ) , whereas hatched g strategies used for protein, the influenza B virus fluenza C virus CMZ .59! es .65 .255on 3me 293.398 3 5339:2003 .mEucmsumm 5305 new mfizmem 8:353 @9523: 3 nos—Ewing don: “$28 @5363 .8533 <zm Ea: vacuum? .595 VGBEl? han...“ mmzm .0 toes . . 528: E 3295 new :2 5.3 2222.: E332 _ m protein. Open boxes ”acct; ‘0 “cocanoo .655. cowloop m—NJ; FNF Nm2 mom oncogene :EotouE use—6o. protein (influenza A and C viruses protein (influenza B virus) appin 520:: new 2:85:25 cocci EVE Ea: (zmun g coding sequences. The CMl ORF is new E3393 5 5905 3582.30: 69.35% :2: .i m5.wm cam 62 8» 0mm a equ on 3:00 weaned IOCBIIOH, runction unknown 8538 <sz 83% I I as N. a ma 25355 .5 3.325 .0555 3538:: was .6. .2233 23:8 .2..ch :2 ”52oz. scenes: 3.9.5 8.8 Se: 8 N5. m5 Nmz Eu #2: £3, neeee £963 Ea: maroon: 62.; 6 £203 Ems. coon 5me mmw :2 moo.— hwo; x. EmEEEeu 2:ng coEgE 53:8 omegsEflzg ”£22833 08:5 oo— “$0.0m vmv <2 won. — n S; w wigs—Sm (2: cat; s new £3553 <21 239:2 2 <sz E0: :8?» E 329E 6.2232038: 3:8 , Eco. 2 <2; 2 8:5 8:68: 89 Beam m2. ".2 8m; mom; m EmEEEEu geomzca SEE 558m :ofiE ecu mucosa _n:o=mE§ceo 305511926. Eozgzum magneto 2588.6 559.3 Eon 23.3 5339 roEE ”sseaouza 8%.; 5.22 com $3.6 mwm 5.. 55 c E: v :2655 sauce "onEoo wmmu=n2 new 339.3%: <zm E EoconEoo colon 8mg m: E San nmmd m xaEEeu :oanEQ new .omflntomcw: <zm B “cocanoo EoEuum 2:523: magnum“. A m @2333 550:3 <sz 7 7 .- .e.a 23E; ”cozfléauuzoo can engage new .n <sz . w W .95 53:8 9535 $322.: w w Eon oEEmim 35 30:55 m .U l u. m M .m d 0 c e .m f 0 W .m d .m t a m e h c S 2 M S u ..II. V A m n c .m :1 .m c h t. f 0 .m S m P a indicate the ORF for the matrix or the neuraminidase boxes indicate overi identical to the gp42 0 NB protein, and the in -_—— A (n) NB NA .—> .—>- AAAAAUGAACAAUGCUA mEoEemamm union new mEoEmmm <2: oEocmu was < «Menace: .F 39:. cDetermined by nucleotide sequence analysis and protein sequencing. “Contribution of carbohydrate makes observed molecular weight larger. “Deduced from FlNA sequence, excluding poly(A) tract. 5.26m ammo—uzcoucm owlon domdm hmh Fwd omn.m Svmd N xeanu n. sugarcane. <zm B .m Eocoquu Jim :3 Go: go Pei. 5538.: 38v :2 exaaawé 8‘8 83m mmh «E can,“ sad F 4 mote—rem :o___> can. 030506 Anny 25:2 oozomnzoa nAmoEBmfiacv Amobzoofiaev EmEmmw % 35020:. is .62 83828 Buoucm 59.5. «£9.04 N t 2 .o: 1055‘ Eoommz (5? P M M N :m I one; \ m<m§>O§EOIEO .ov , after which a stop . RF until amino acid 242 codon introduced by the splice junction terminates the ORF. Orthomyxoviridae (influenza virus)! RNA ‘?fii zgmmi @Schematic diagram to illustrate the differences between influenza virus virion FINA (vFlNA) seg- ments, mRNAs and full-length cRNA or template RNA. The conserved 12 nucleotides at the 3' end and 3 13 nucleotides at the 5' end of each influenza A virus vRNA segment are indicated. The mRNAs con- 1 CAP-BINDING tain a m’Gppr'“ cap structure and on average 10 to 13 nucleotides derived lrorn a subset ot host cell . ACTIVATED RNAs (see Fig. 16 and text). Polyadenylation ot the mFtNAs occurs at a site 15 to 22 nucleotides before i the 5' and ot the thNA segment. The template RNA contains at its 5' terminus pppA and it is a complete ! copy of the vRNA segment. Redrawn from Lamb and Choppin (211). vRNA . (C E! ) 3ucecuuuccucc ——-——/ /———e—— GGMCMAGAUGA we 5 ‘ O——'”“"‘——--- u 5'cm’ 5- mRNA® 3‘ m7cpppx'“ Y ........... AGCGAAAGCAGG ————/ ,L—— Am) @ L EA |‘——— 15- 22 ——-—-I ENDONUCLEASE ‘°‘3 ACHVATED Nucleotides Nucleotides 34w 5. template R a- pppAGCGAAAGCAGG ————1’/‘—-—— CCUUGUUUCUACU A MATURE . TRANSCRIPTION COMPLEX if . i tmnAnon 3 ' 7‘ n = e ‘ " u . 1: . s .3: z .e 2 $2 Sig a: s a s A 2 ~ 0 :: a s l ~ss 0mA<_N 23- as. me 2 I E < 8. U) 3E '0 ,‘_- I 3 E I d) 53 W l I a" U" 4- q) '- l w v 3E l E .g It, 3 £33,: 2 i o > N a: a) at LL, :9 2 In 13 c .1: . ELONGATION in (0 E 'E O .- a ' I a D '61 “‘ no N Vewgfiv ( 8 0,12 0- : 2 I =Et=91 .. .t: - 3 (l1 5 . e 9 ya t g at 3 a (250:5 = I n 0-1: I 2 5 E " o O E H-c f: ._ c o 3 ~ 5 ‘s = 3 a E = 9 ° ,. 2 c “ on: 0 : e .. a o .— c u .2 < : 2 -; o 2 < 2 ° 16 2 e g z 9 w- I a 13 I: D I > o : t: t: o '5 3' 3 ° C '1’ c' ‘5 {7:3 :85 oEBAwm : a, a, 0 Q >.= 4 E s :3 fi .2 n a 3 E a 39 ° 3 3 . "' n no: 3 ° «1 5 . POLYADENYLATION fig<=3n 9 < I I: o (9 CA I S a s s as; .1, 55m§<z 33 writ, WIRNA® -= (D f: m I 3 “amass :5, 3 8 ‘8’ E E FIG. 16. Model tor assembly of the polymerase complex and subsequent viral transcription. A: The three '- 0,2 '6 3 5 3 polymerase proteins assemble initially into an inactive complex. 1. Upon binding to the 5' and sequence ‘ E 0 a 'a w- 3. of vRNA, mFINA cap-binding activity associated with the P82 subunit is acquired. 2. Interaction with the I 3 .9 a E ‘8 x 3’ and ot vRNA activates the endonuclease activity oi the polymerase complex. This can occur prior to g 55 o 3 g or subsequent to binding to the capped mRNA primer. Cleavage of the capped mFtNA then occurs. cre- rn 8 E E ‘5 5 ating a mature transcription complex. Data from Ciana et al. (59). B: Initiation usually occurs at the penul- E ‘5 E f, g 0 timate base and transcription then proceeds as the 3’ ends of vFINAs thread through the polymerase g a}; g o g complex. The 5' end sequences of vFlNA remains tightly bound to the polymerase throughout tran- g._ 5 a: 5 H :- scription. The cap structure initially remains bound to the P82 subunit, but becomes disengaged soon 5 O E 2 ,,, "5 0 after elongation ensues. Polyadenylation occurs upon encountering the oligo U sequence adjacent to _ g a g ‘T c g the 5' end through a slippage mechanism. as the polymerase bound to the 5' and does not allow read- “ "r7: 5 g E .9 _ through. Courtesy of L. Tiley and M. Krystal, Bristol-Meyers Squibb Pharmaceutical Research Institute. daagzo§wwWM£1 _. c n. o o g o u. i— to n .o u— o. ...
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