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We propose that PILRA G78R protects individuals from Alzheimer's disease risk via reduced inhibitory signaling in microglia and reduced microglial infection during HSV-1 recurrence.
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Data suggest that, although PILRA exhibits essentially the same recognition of different glycopeptides, slight modifications of linker sugar cause significant changes in a wide area of the binding interface, resulting in a reduction of binding affinity; analogs/fragments of gpb were used in these studies. (PILRA = paired immunoglobin like type 2 receptor alpha; gpb = envelope glycoprotein B, Herpes simplex virus type 1)
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The interaction of NK cells with PILRalpha expressing targets lead to elevated IFNgamma secretion and cytotoxicity. In conclusion, PILRalpha is a novel NK activating ligand which binds and activates an unknown NK receptor expressed on a unique NK cell subset.
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Transcriptome wide association study results identified two novel genes as statistically significantly associated with nonobstructive azoospermia susceptibility: PILRA and ZNF676.
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PILRalpha exhibits large conformational change to recognize simultaneously both the sTn O-glycan and the compact peptide structure constrained by proline residues
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These results contribute our knowledge of the biological functions of HBVDNAPTP1 and provide novel data to aid in the further analysis of the regulatory mechanism of this protein.
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We demonstrated that three residues (Y2, R95, and W108) presented on the surface of PILRalpha form the sialic acid binding site equivalent to those in siglecs but are arranged in a unique linear mode.
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The amino terminus of herpes simplex virus 1 gK is functionally and physically associated with the gB-PILRalpha protein complex and regulates membrane fusion of the viral envelope with cellular membranes during virus entry.
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The authors show that the human ocular and highly neurovirulent HSV-1 strain McKrae enters substantially more efficiently into cells via the gB-specific human paired immunoglobulin-like type-2 receptor-alpha (hPILR-alpha).
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Data show that PILRalpha/ligand interactions require conserved PILRalpha arginine (Arg)-133 (mouse) and Arg-126 (human).
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These results suggest that PANP is involved in immune regulation as a ligand of the PILRalpha.
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PILRalpha protein was successfully crystallized at 293 K using the sitting-drop vapour-diffusion method and the crystals diffracted to 1.3 A resolution.
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The results demonstrate that cellular receptors for both gB and gD are required for HSV-1 infection and that PILRalpha plays an important role in HSV-1 infection as a coreceptor that associates with gB.
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viral entry via PILRalpha appears to be conserved but that there is a PILRalpha preference among alphaherpesviruses
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Insertional mutations of gB reduced cell fusion activity when PILRalpha was overexpressed much more than nectin-1.
