Encephalomyocarditis Virus Leader Is Phosphorylated by CK2 and Syk as a Requirement for Subsequent Phosphorylation of Cellular Nucleoporins

Basta, Holly A.; Bacot‐Davis, Valjean R.; Ciomperlik, Jessica J.; Palmenberg, Ann C.

doi:10.1128/jvi.03150-13

Cited by 15 publications

(40 citation statements)

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“…This inhibition happens in infected cells even before the virus begins to replicate (6,26). The cascade involves Erk1/2 and p38 kinases and is absolutely dependent on Ran:L E interactions and also on the dual phosphorylation of L E itself, an activity that is a prerequisite, and not a consequence, of the Nup modifications (7,10,15,16,27). Furthermore, the L E zinc finger motif must remain intact and chelated to the metal for the protein to function (11).…”

Section: Discussionmentioning

confidence: 99%

“…Although compressed topology was the most noticeable structural characteristic of progressive L M phosphorylation, in none of the states, for any of the proteins, was there evidence of direct interactions among the defined phenotypic domains. Notably, however, L M phosphorylation did affect residue H 16 Table 1. Tables S2 and S3 record determined values for distance restraint reliabilities and structure quality.…”

Section: Significancementioning

confidence: 99%

“…All these tails (RMSD, 4.9 Å) had the same central helix (aa 196-206), but none were similarly oriented relative to the core. Among Ran structures solved by crystallography, the COOH tail arrangements can vary according to nucleotide status and binding partner-induced shifts that may also involve the nucleotideproximal phosphate binding P-loop (aa [16][17][18][19][20][21][22][23][24][25], Switch 1 (aa 32-45), Switch 2 (aa 66-79), and basic patch (aa 139-142) internal core segments (Fig. 3) …”

Section: Significancementioning

confidence: 99%

“…In the residue numbering for recombinant L M (native +4), the zinc finger (aa 14-26), hinge region (aa 35-45), and acidic domain (aa 41-65) form phenotypic landmarks defined by mutagenesis studies (15). T 51 and Y 45 are the phosphorylation sites (16). When L M 0P, L M 1P, and L M 2P were superimposed, the overall root mean square deviation (RMSD) was 12.8 Å for all backbone atoms.…”

Section: Significancementioning

confidence: 99%

“…1A). The change is in a conserved, amino-proximal CHCC zinc finger motif (aa [10][11][12][13][14][15][16][17][18][19][20][21][22], the structure of which was determined by NMR for the L M protein (14). Technical difficulties hampered resolution of the complete protein, but a full coordinate set was recently completed [Protein Data Bank (PDB) ID code 2M7Y].…”

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confidence: 99%

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Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase

Bacot‐Davis

Ciomperlik

Basta

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Cardiovirus Leader (L) proteins induce potent antihost inhibition of active cellular nucleocytoplasmic trafficking by triggering aberrant hyperphosphorylation of nuclear pore proteins (Nup). To achieve this, L binds protein RanGTPase (Ran), a key trafficking regulator, and diverts it into tertiary or quaternary complexes with required kinases. The activity of L is regulated by two phosphorylation events not required for Ran binding. Matched NMR studies on the unphosphorylated, singly, and doubly phosphorylated variants of Mengovirus L (L M ) show both modifications act together to partially stabilize a short internal α-helix comprising L M residues 43-46. This motif implies that ionic and Van der Waals forces contributed by phosphorylation help organize downstream residues 48-67 into a new interface. The full structure of L M as bound to Ran (unlabeled) and Ran (216 aa

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Section: Discussionmentioning

confidence: 99%

Section: Significancementioning

confidence: 99%

Section: Significancementioning

confidence: 99%

Section: Significancementioning

confidence: 99%

mentioning

confidence: 99%

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Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase

Bacot‐Davis

Ciomperlik

Basta

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Nucleoporins in Retroviral Replication

Monette

Mouland

2018

Retrovirus-Cell Interactions

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Induction and suppression of innate antiviral responses by picornaviruses

Qian

Langereis

Kuppeveld

2014

Cytokine & Growth Factor Reviews

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Cover illustrationsThis thesis has a strong emphasis on the battle between viruses and their hosts -how the host recognizes the enemy, and how the virus tries to evade the host defense system. However, it is not to be forgotten that viruses and their hosts have also come to an agreement, or a common understanding, if you like, during their very long co-evolution. Viruses do not wipe off their host species, and the host also lends resources to allow the virus to replicate, once in a while. Cover designed by Qian FengCover executed by Nikki Vermeulen, Ridderprint BV Printed byRidderprint BV, Ridderkerk, The Netherlands Printing of this thesis was partially sponsored by Graduate School Infection & Immunity Utrecht Copyright 2014 Qian FengAll rights reserved. No part of this publication may be reproduced or transmitted in any form or by any means without written permission of the author and the publisher holding the copyrights of the published articles. ISBN 978-90-393-6160-3Proefschrift Versie 1. Chapter 1 General IntroductionProefschrift Versie 1.indd 9 18-5-2014 18:31:54Chapter 1 10 PICORNAVIRUSES Viral diseases have long accompanied mankind. An ancient Egyptian stele dated to 1403-1365 BC depicts a man with a withered leg, a symptom rather typical to that of poliomyelitis caused by poliovirus (PV), may very well be one of the earliest documentations of a viral disease (1). Picornaviridae is a large family of human and animal pathogens comprising of 17 genera, including Enterovirus, Cardiovirus, Parechovirus, and Aphthovirus. These viruses were traditionally classified based on their pathogenicity in humans and animals, and defined as serotypes. However, with increasing advancements in sequence analysis, picornaviruses are currently grouped based on their genetic relationships. For instance, many coxsackievirus A (CVA) serotypes are split into the species Enterovirus A and C, and species Enterovirus B contains many CVB serotypes and many echoviruses. Furthermore, rhinoviruses, which cause pathology in the respiratory systems, were initially recognized as a separate genus, but have been grouped into the Enterovirus genus since their genomic sequences are known. Figure 1 represents the classification of picornaviruses according to the International Committee of Taxonomy of Viruses (ICTV) as of 28 February, 2014, specially featuring the genera Enterovirus and Cardiovirus.Among the large picornavirus family, the Enterovirus genus contains a large number of human pathogens. PV is the etiological agent of the paralytic disease poliomyelitis and caused large scale epidemics worldwide prior to the introduction of vaccines in the late 1950's and early 1960's, which tremendously helped to keep poliovirus under control in developed countries, but it continues to cause outbreaks in parts of the world even today. Since 1988, PV has become the subject of a global eradication campaign launched by the WHO, a multibillion dollar international operation that was intended to end in 2000 but is still not completed in 2014 (1). Othe...

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Encephalomyocarditis Virus Leader Is Phosphorylated by CK2 and Syk as a Requirement for Subsequent Phosphorylation of Cellular Nucleoporins

Abstract: Encephalomyocarditis virus and

Cited by 15 publications

References 44 publications

Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase

Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase

Nucleoporins in Retroviral Replication

Induction and suppression of innate antiviral responses by picornaviruses

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