Cryo-EM structure of enteric adenovirus HAdV-F41 highlights
structural variations among human adenoviruses

J 2021

Cryo-EM structure of enteric adenovirus HAdV-F41 highlights structural variations among human adenoviruses

PEREZ-ILLANA, M., M. MARTINEZ, G.N. CONDEZO, M. HERNANDO-PEREZ, C. MANGROO et. al.

Základní údaje

Originální název

Cryo-EM structure of enteric adenovirus HAdV-F41 highlights structural variations among human adenoviruses

Autoři

PEREZ-ILLANA, M., M. MARTINEZ, G.N. CONDEZO, M. HERNANDO-PEREZ, C. MANGROO, M. BROWN, R. MARABINI a C. SAN MARTIN

Vydání

Science advances, New York, American Association for the Advancement of Science, 2021, 2375-2548

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 14.957

Kód RIV

RIV/00216224:14740/21:00124439

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1126/sciadv.abd9421

UT WoS

000622481300021

Klíčová slova anglicky

Coat proteins; Enteric adenovirus; Human adenovirus; Oral delivery; Resolution structure; Structural variations

Štítky

CF CRYO, ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 23. 3. 2022 12:02, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Enteric adenoviruses, one of the main causes of viral gastroenteritis in the world, must withstand the harsh conditions found in the gut. This requirement suggests that capsid stability must be different from that of other adenoviruses. We report the 4-angstrom-resolution structure of a human enteric adenovirus, HAdV-F41, and compare it with that of other adenoviruses with respiratory (HAdV-C5) and ocular (HAdV-D26) tropisms. While the overall structures of hexon, penton base, and internal minor coat proteins IIIa and VIII are conserved, we observe partially ordered elements reinforcing the vertex region, which suggests their role in enhancing the physicochemical capsid stability of HAdV-F41. Unexpectedly, we find an organization of the external minor coat protein IX different from all previously characterized human and nonhuman mastadenoviruses. Knowledge of the structure of enteric adenoviruses provides a starting point for the design of vectors suitable for oral delivery or intestinal targeting.

Návaznosti

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

PEREZ-ILLANA, M., M. MARTINEZ, G.N. CONDEZO, M. HERNANDO-PEREZ, C. MANGROO, M. BROWN, R. MARABINI a C. SAN MARTIN. Cryo-EM structure of enteric adenovirus HAdV-F41 highlights structural variations among human adenoviruses. Science advances. New York: American Association for the Advancement of Science, 2021, roč. 7, č. 9, s. 1-14. ISSN 2375-2548. Dostupné z: https://dx.doi.org/10.1126/sciadv.abd9421.

@article{1842608,
   author = {PerezandIllana, M. and Martinez, M. and Condezo, G.N. and HernandoandPerez, M. and Mangroo, C. and Brown, M. and Marabini, R. and San Martin, C.},
   article_location = {New York},
   article_number = {9},
   doi = {http://dx.doi.org/10.1126/sciadv.abd9421},
   keywords = {Coat proteins; Enteric adenovirus; Human adenovirus; Oral delivery; Resolution structure; Structural variations},
   language = {eng},
   issn = {2375-2548},
   journal = {Science advances},
   title = {Cryo-EM structure of enteric adenovirus HAdV-F41 highlights structural variations among human adenoviruses},
   url = {https://www.science.org/doi/10.1126/sciadv.abd9421},
   volume = {7},
   year = {2021}
}

TY  - JOUR
ID  - 1842608
AU  - Perez-Illana, M. - Martinez, M. - Condezo, G.N. - Hernando-Perez, M. - Mangroo, C. - Brown, M. - Marabini, R. - San Martin, C.
PY  - 2021
TI  - Cryo-EM structure of enteric adenovirus HAdV-F41 highlights structural variations among human adenoviruses
JF  - Science advances
VL  - 7
IS  - 9
SP  - 1-14
EP  - 1-14
PB  - American Association for the Advancement of Science
SN  - 23752548
KW  - Coat proteins
KW  - Enteric adenovirus
KW  - Human adenovirus
KW  - Oral delivery
KW  - Resolution structure
KW  - Structural variations
UR  - https://www.science.org/doi/10.1126/sciadv.abd9421
N2  - Enteric adenoviruses, one of the main causes of viral gastroenteritis in the world, must withstand the harsh conditions found in the gut. This requirement suggests that capsid stability must be different from that of other adenoviruses. We report the 4-angstrom-resolution structure of a human enteric adenovirus, HAdV-F41, and compare it with that of other adenoviruses with respiratory (HAdV-C5) and ocular (HAdV-D26) tropisms. While the overall structures of hexon, penton base, and internal minor coat proteins IIIa and VIII are conserved, we observe partially ordered elements reinforcing the vertex region, which suggests their role in enhancing the physicochemical capsid stability of HAdV-F41. Unexpectedly, we find an organization of the external minor coat protein IX different from all previously characterized human and nonhuman mastadenoviruses. Knowledge of the structure of enteric adenoviruses provides a starting point for the design of vectors suitable for oral delivery or intestinal targeting.
ER  -

PEREZ-ILLANA, M., M. MARTINEZ, G.N. CONDEZO, M. HERNANDO-PEREZ, C. MANGROO, M. BROWN, R. MARABINI a C. SAN MARTIN. Cryo-EM structure of enteric adenovirus HAdV-F41 highlights structural variations among human adenoviruses. \textit{Science advances}. New York: American Association for the Advancement of Science, 2021, roč.~7, č.~9, s.~1-14. ISSN~2375-2548. Dostupné z: https://dx.doi.org/10.1126/sciadv.abd9421.

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