4.3 Review

Viral calciomics: Interplays between Ca2+ and virus

Journal

CELL CALCIUM
Volume 46, Issue 1, Pages 1-17

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.ceca.2009.05.005

Keywords

Virus; Calcium; Signaling; EF-hand; Structure; Interaction; Apoptosis; Infection

Categories

Funding

  1. NIAID [R01 AI21389]
  2. NIH [R01 GM 62999]
  3. NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI021389] Funding Source: NIH RePORTER
  4. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM062999] Funding Source: NIH RePORTER

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Ca2+ is one of the most universal and versatile signaling molecules and is involved in almost every aspect of cellular processes. Viruses are adept at utilizing the universal Ca2+ signal to create a tailored cellular environment that meets their own demands. This review summarizes most of the known mechanisms by which viruses perturb Ca2+ homeostasis and utilize Ca2+ and cellular Ca2+-binding proteins to their benefit in their replication cycles. Ca2+ plays important roles in virion structure formation, virus entry, viral gene expression, posttranslational processing of viral proteins and virion maturation and release. As part of the review, we introduce an algorithm to identify linear EF-hand Ca2+-binding motifs which resulted in the prediction of a total of 93 previously unrecognized Ca2+-binding motifs in virus proteins. Many of these proteins are nonstructural proteins, a class of proteins among which Ca2+ interactions had not been formerly appreciated. The presence of linear Ca2+-binding motifs in viral proteins enlarges the spectrum of Ca2+-virus interplay and expands the total scenario of viral calciomics. (C) 2009 Elsevier Ltd. All rights reserved.

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