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Megavirus chilensis

Come leggere il tassoboxProgetto:Forme di vita/Come leggere il tassobox
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Classificazione scientifica
DominioVaridnaviria
RegnoBamfordvirae
PhylumNucleocytoviricota
ClasseMegaviricetes
OrdineImitevirales
FamigliaMimiviridae
GenereMegavirus
SpecieMegavirus chilensis

Il Megavirus chilensis è una specie di virus appartenente al genere Megavirus.[1]

Storia

Venne scoperto in un campione d'acqua proveniente dall'oceano Pacifico, al largo delle coste cilene.[2]

Descrizione

Il virione è costituito da un capside icosaedrico di 400 nm di diametro racchiuso in uno strato di fibrilla.[3]

Genetica

Presenta un genoma composto da DNA a doppia elica di 1.259 Mb che codifica 1.120 geni ricco in adenina e timina (75% A+T).[1] Di questi circa 600 sono comuni a quelli del Mimivirus con una media del 50% di residui identici a livello della sequenza proteica.[2][1] Il virus mantiene le qualità e le caratteristiche genomiche del Mimivirus a cui si aggiungono tre geni codificanti altrettante aminoacil-tRNA sintetasi (IleRS, TrpRS, AsnRS).[2]

Nella sequenza è presente il gene Mg277 che codifica la superossido dismutasi rame e zinco (Cu,Zn-SOD), come alcuni membri della stessa famiglia e a differenza del Mimivirus, presente nelle particelle purificate del virione.[4]

La superossido dismutasi rame e zinco catalizza la conversione di radicali superossidi a perossido d'idrogeno e diossidi. Si tratta di un enzima dimerico che presenta un ponte disolfuro, la cui integrità strutturale è mantenuta dagli atomi di zinco,[5] mentre il rame è il cofattore catalitico.[6] Ha il compito di detossificare le specie ossigenate rilasciate dall'ospite come meccanismo di difesa. Omologhi sono presenti nei megavirus e nei moumouvirus, con un 77% - 90% di residui identici, ovvero nei baculovirus, nei clorovirus e nei poxvirus.[7]

L'enzima legato risulta iperstabile con una temperatura di fusione misurata di 76°C, mentre in forma libera la sua temperatura di fusione risulta inferiore (56°C).[7] In ciascun monomero, un residuo glutamminico contribuisce fortemente all'interfaccia dimerica mediante due legami a idrogeno che collegano due residui Q116.[8]Il ponte disolfuro aumenta e i due legami a idrogeno, sono probabilmente responsabili dell'iperstabilità della proteina legata.[7]

Biologia

Il virus è in grado di replicarsi in specie del genere Acanthamoeba che vivono in acqua dolce.[2]

Note

  1. ^ a b c (EN) Matthieu Legendre, Defne Arslan e Chantal Abergel, Genomics of Megavirus and the elusive fourth domain of Life, in Communicative & Integrative Biology, vol. 5, n. 1, 2012-01, pp. 102–106, DOI:10.4161/cib.18624. URL consultato il 20 giugno 2024.
  2. ^ a b c d (EN) Defne Arslan, Matthieu Legendre e Virginie Seltzer, Distant Mimivirus relative with a larger genome highlights the fundamental features of Megaviridae, in Proceedings of the National Academy of Sciences, vol. 108, n. 42, 18 ottobre 2011, pp. 17486–17491, DOI:10.1073/pnas.1110889108. URL consultato il 20 giugno 2024.
  3. ^ (EN) Audrey Lartigue, Bénédicte Burlat e Bruno Coutard, The Megavirus Chilensis Cu,Zn-Superoxide Dismutase: the First Viral Structure of a Typical Cellular Copper Chaperone-Independent Hyperstable Dimeric Enzyme, in G. McFadden (a cura di), Journal of Virology, vol. 89, n. 1, 2015-01, pp. 824–832, DOI:10.1128/JVI.02588-14. URL consultato il 20 giugno 2024.
  4. ^ Audrey Lartigue, Nadège Philippe e Sandra Jeudy, Preliminary crystallographic analysis of the Megavirus superoxide dismutase, in Acta Crystallographica Section F Structural Biology and Crystallization Communications, vol. 68, n. 12, 1º dicembre 2012, pp. 1557–1559, DOI:10.1107/S174430911204657X. URL consultato il 20 giugno 2024.
  5. ^ Marmocchi F, Caulini G, Venardi G, Cocco D, Calabrese L, Rotilio G., The effect of the presence of the metal prosthetic groups on the subunit structure of bovine superoxide dismutase in sodium dodecyl sulfate., in Physiol Chem Phys, vol. 7, 1975, pp. 465–471.
  6. ^ Dina Klug, Joseph Rabani e Irwin Fridovich, A Direct Demonstration of the Catalytic Action of Superoxide Dismutase through the Use of Pulse Radiolysis, in Journal of Biological Chemistry, vol. 247, n. 15, 1972-08, pp. 4839–4842, DOI:10.1016/s0021-9258(19)44987-9. URL consultato il 20 giugno 2024.
  7. ^ a b c (EN) Audrey Lartigue, Bénédicte Burlat e Bruno Coutard, The Megavirus Chilensis Cu,Zn-Superoxide Dismutase: the First Viral Structure of a Typical Cellular Copper Chaperone-Independent Hyperstable Dimeric Enzyme, in G. McFadden (a cura di), Journal of Virology, vol. 89, n. 1, 2015-01, pp. 824–832, DOI:10.1128/JVI.02588-14. URL consultato il 20 giugno 2024.
  8. ^ (EN) Zheng You, Xiaohang Cao e Alexander B. Taylor, Characterization of a Covalent Polysulfane Bridge in Copper−Zinc Superoxide Dismutase,, in Biochemistry, vol. 49, n. 6, 16 febbraio 2010, pp. 1191–1198, DOI:10.1021/bi901844d. URL consultato il 20 giugno 2024.

Voci correlate

Altri progetti

Collegamenti esterni

  • Struttura della superossido dismutasi rame e zinco di M. chilensis in RCSB PDB
  Portale Microbiologia: accedi alle voci di Wikipedia che trattano di microbiologia

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