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.

Basic information

Original name

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

Authors

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

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 14.957

RIV identification code

RIV/00216224:14740/21:00124439

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

000622481300021

Keywords in English

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

Abstract

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.

Links

90127, large research infrastructures

Name: CIISB II

Citovat

PEREZ-ILLANA, M., M. MARTINEZ, G.N. CONDEZO, M. HERNANDO-PEREZ, C. MANGROO, M. BROWN, R. MARABINI and 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, vol. 7, No 9, p. 1-14. ISSN 2375-2548. Available from: 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 and 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, vol.~7, No~9, p.~1-14. ISSN~2375-2548. Available from: https://dx.doi.org/10.1126/sciadv.abd9421.

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