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Virology. 2019 Aug;534:45-53. doi: 10.1016/j.virol.2019.05.021. Epub 2019 Jun 2.

Of capsid structure and stability: The partnership between charged residues of E-loop and P-domain of the bacteriophage P22 coat protein.

Author information

1
Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT, USA.
2
Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT, USA; Department of Chemistry, University of Connecticut, Storrs, CT, USA. Electronic address: carolyn.teschke@uconn.edu.

Abstract

Tailed dsDNA bacteriophages and herpesviruses form capsids using coat proteins that have the HK97 fold. In these viruses, the coat proteins first assemble into procapsids, which subsequently mature during DNA packaging. Generally interactions between the coat protein E-loop of one subunit and the P-domain of an adjacent subunit help stabilize both capsomers and capsids. Based on a recent 3.3 Å cryo-EM structure of the bacteriophage P22 virion, E-loop amino acids E52, E59 and E72 were suggested to stabilize the capsid through intra-capsomer salt bridges with the P-domain residues R102, R109 and K118. The glutamic acid residues were each mutated to alanine to test this hypothesis. The substitutions resulted in a WT phenotype and did not destabilize capsids; rather, the alanine substituted coat proteins increased the stability of procapsids and virions. These results indicate that different types of interactions must be used between the E-loop and P-domain to stabilize phage P22 procapsids and virions.

KEYWORDS:

Capsid stability; Phage burst; Titer; Urea titration; Virus structure

PMID:
31176063
PMCID:
PMC6614003
[Available on 2020-08-01]
DOI:
10.1016/j.virol.2019.05.021

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