Abstract
Glycoprotein L (gL) is one of the critical proteins involved in transmission of Herpesviridae. We applied the methodology of protein structure prediction to shed a light on the so far unknown molecular mechanism of its action. Here we show that gL forms a chemokine-like protein. Alphaherpesvirinae gL as well as CMV functional homolog (UL130) create a novel CX chemokine-like protein, while Gammaherpesvirinae gL (HHV8 and EBV) adopt a regular CC beta-chemokine fold. We conclude that gL may interact with specific cellular chemokine receptors during the invasion of Herpesviridae. The proposed mechanism has a potential impact on future development of novel therapeutic and prophylactic strategies.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Conserved Sequence
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Cysteine / chemistry
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Databases, Genetic
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Databases, Protein
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Disulfides / chemistry
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Glycoproteins / chemistry*
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Glycoproteins / genetics
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Herpesviridae / chemistry*
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Herpesviridae / genetics
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Herpesviridae / pathogenicity
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Hydrophobic and Hydrophilic Interactions
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Ligands
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Models, Chemical
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Molecular Sequence Data
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Protein Structure, Secondary
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Receptors, Chemokine / chemistry*
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Receptors, Chemokine / genetics
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Sequence Analysis, Protein
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Sequence Homology, Amino Acid
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Viral Proteins / chemistry*
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Viral Proteins / genetics
Substances
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Disulfides
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Glycoproteins
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Ligands
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Receptors, Chemokine
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Viral Proteins
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Cysteine