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Fig. 2 HAdV-D26K shares key binding residues with sialic acid–using adenoviruses and exploits sialic acid to infect cells. HAdV-D26K shares key binding.

Published byŌἈμώς Ιωάννου Modified over 5 years ago

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Presentation on theme: "Fig. 2 HAdV-D26K shares key binding residues with sialic acid–using adenoviruses and exploits sialic acid to infect cells. HAdV-D26K shares key binding."— Presentation transcript:

1 Fig. 2 HAdV-D26K shares key binding residues with sialic acid–using adenoviruses and exploits sialic acid to infect cells. HAdV-D26K shares key binding residues with sialic acid–using adenoviruses and exploits sialic acid to infect cells. (A) Sequence alignment of HAdV-D26K shows conservation of key binding residues with known sialic acid–binding adenoviruses; top numbering is according to HAdV-D26K. Residues boxed in red form polar contacts with sialic acid, those boxed in black denote contact sialic acid via water bridge, and those boxed in orange indicate hydrophobic contacts; all HAdV-D26K polar contacts also form water bridges. Neuraminidase treatment does not reduce the ability of HAdV-D5/B35K (B) or HAdV-C5 (C) to infect SKOV-3 (ovarian adenocarcinoma), BT-20 (breast carcinoma), or MDA-231 (metastatic breast adenocarcinoma) cells, while HAdV-D5/D26K (D) is significantly inhibited. n = 3 biological replicates; error bars indicate ±SD. Alexander T. Baker et al. Sci Adv 2019;5:eaax3567 Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY).

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