Structure-based assessment of protein-protein interactions and accessibility of protein IX in adenoviruses with implications for antigen display

Nathaniel L. Matteson, Michael A Barry, Vijay S. Reddy

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The exterior minor protein IX of adenoviruses (AdVs) is a frequent target of attachment of antigens and the modified AdVs are being used as potent vaccine platforms. The organization of protein IX is disticntly different between human adenoviruses (HAdVs) and non-HAdVs. The analysis of solvent accessibility, based on the near atomic resolution structures, suggests that the C-terminal residues of IX are more accessible in non-HAdVs (e.g., bovine adenovirus) than in HAdVs. Although the C-terminal fusions of IX are displayed on the capsid surface, they could disrupt the formation of tetrameric coiled-coils (4-HLXB) in HAdVs due to steric hinderance, thereby potentially affecting the capsid stability. Importantly, the parallel-antiparallel arrangement of helices seen in the 4-HLXB is not condusive for IX C-terminal fusions in HAdVs. In contrast, the parallel trimeric C-terminal coiled-coils in non-HAdVs are unlikely to be affected by the attachment of antigens and more efficiently displayed on the AdV surface.

Original languageEnglish (US)
Pages (from-to)102-107
Number of pages6
JournalVirology
Volume516
DOIs
StatePublished - Mar 1 2018

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Adenoviridae
Human Adenoviruses
Antigens
Proteins
Capsid
Vaccines

Keywords

  • Adenoviruses
  • Peptide attachements and antigen display
  • Protein IX
  • Protein network
  • Structure

ASJC Scopus subject areas

  • Virology

Cite this

Structure-based assessment of protein-protein interactions and accessibility of protein IX in adenoviruses with implications for antigen display. / Matteson, Nathaniel L.; Barry, Michael A; Reddy, Vijay S.

In: Virology, Vol. 516, 01.03.2018, p. 102-107.

Research output: Contribution to journalArticle

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