ArticlebioRxiv : the preprint server for biology2025
The human cytomegalovirus chemokine binding protein UL22A is necessary for efficient reactivation from latency in CD34
Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Herpesviruses and Poxviruses encode secreted chemokine binding proteins that prevent the interaction between chemokines and their cognate G protein coupled receptors to alter chemotactic gradients and intracellular signaling pathways. Human cytomegalovirus (HCMV) encodes the secreted protein UL22A (formerly UL21.5), which is described as a CCL5 (RANTES) binding protein and requires sulfation at two tyrosine residues (Y65 and Y69) for efficient RANTES interaction. In this report, we show that the UL22A protein, and the UL22A Y65 and Y69 residues are necessary for efficient HCMV reactivation from latency in CD34 IMPORTANCE: HCMV is a ubiquitous herpesvirus that infects 60-90% of the population worldwide. In immunocompetent individuals, primary infection is asymptomatic and results in lifelong latent infection in CD34
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