5VX9

VP8* of P[6] Human Rotavirus RV3 in complex with LNFP1

Summary for 5VX9

• Entry DOI: 10.2210/pdb5vx9/pdb
• Descriptor: Outer capsid protein VP4, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• Functional Keywords: glycan, hbga, rotavirus, viral protein
• Biological source: Human rotavirus A
• Total number of polymer chains: 1
• Total formula weight: 19529.37

Authors

Hu, L.,Venkataram Prasad, B.V. (deposition date: 2017-05-23, release date: 2018-07-18, Last modification date: 2023-10-04)

Primary citation

Hu, L.,Sankaran, B.,Laucirica, D.R.,Patil, K.,Salmen, W.,Ferreon, A.C.M.,Tsoi, P.S.,Lasanajak, Y.,Smith, D.F.,Ramani, S.,Atmar, R.L.,Estes, M.K.,Ferreon, J.C.,Prasad, B.V.V.
Glycan recognition in globally dominant human rotaviruses.
Nat Commun, 9:2631-2631, 2018

PubMed Abstract: Rotaviruses (RVs) cause life-threatening diarrhea in infants and children worldwide. Recent biochemical and epidemiological studies underscore the importance of histo-blood group antigens (HBGA) as both cell attachment and susceptibility factors for the globally dominant P[4], P[6], and P[8] genotypes of human RVs. How these genotypes interact with HBGA is not known. Here, our crystal structures of P[4] and a neonate-specific P[6] VP8*s alone and in complex with H-type I HBGA reveal a unique glycan binding site that is conserved in the globally dominant genotypes and allows for the binding of ABH HBGAs, consistent with their prevalence. Remarkably, the VP8* of P[6] RVs isolated from neonates displays subtle structural changes in this binding site that may restrict its ability to bind branched glycans. This provides a structural basis for the age-restricted tropism of some P[6] RVs as developmentally regulated unbranched glycans are more abundant in the neonatal gut.

PubMed: 29980685
DOI: 10.1038/s41467-018-05098-4

Experimental method

X-RAY DIFFRACTION (1.822 Å)