Revisiting the role of histo-blood group antigens in rotavirus host-cell invasion

Böhm, Raphael; Fleming, Fiona E.; Maggioni, Andrea; Dang, Vi; Holloway, Gavan; Coulson, Barbara S.; Itzstein, Mark von; Haselhorst, Thomas

doi:10.1038/ncomms6907

Cited by 80 publications

(131 citation statements)

References 69 publications

(113 reference statements)

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“…P [19] is a rare RVA P genotype reported in humans and pigs (4). It was found to be combined with various G genotypes (23).…”

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confidence: 99%

“…In addition, P [9], P [14], and P [25] all bound to A type HBGA (A-HBGA) (18). Using saturation transfer difference nuclear magnetic resonance (STD-NMR), DS-1 P [4], RV-3 P [6], ST-3 P [6], and HAL1141 P [14] RVs were shown to bind to A-HBGA, whereas Wa P [8] did not (19). In addition, the VP8* protein of Wa also showed no binding to H1 or [6], and P [8]) are all clustered in P [II].…”

mentioning

confidence: 99%

“…It was found to be combined with various G genotypes (23). P [19] was first identified in pigs in 1986 (4F) (24). The first human P [19] RV strains were detected in Thailand in 1989 (Mc323 and Mc345) (25).…”

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confidence: 99%

“…P [19] was first identified in pigs in 1986 (4F) (24). The first human P [19] RV strains were detected in Thailand in 1989 (Mc323 and Mc345) (25). Whole-genome analysis revealed that human P [19] RV Mc323 and Mc345 were of porcine origin (26).…”

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confidence: 99%

“…The first human P [19] RV strains were detected in Thailand in 1989 (Mc323 and Mc345) (25). Whole-genome analysis revealed that human P [19] RV Mc323 and Mc345 were of porcine origin (26). It is unknown whether P [19] has HBGA binding patterns similar to those of other members of the P[II] genogroup (P[4]/P [8] or P [6]), which may be essential for understanding P [19] RV infection and transmission in humans and pigs.…”

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confidence: 99%

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Functional and Structural Characterization of P[19] Rotavirus VP8* Interaction with Histo-blood Group Antigens

Sun

Peng

et al. 2016

J Virol

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Rotaviruses (RVsR otaviruses (RVs) are the major causative agents of acute gastroenteritis in young children and animals worldwide (1). The RV genome contains 11 segments of double-stranded RNA encoding 12 proteins: six structural proteins (VP1, VP2, VP3, VP4, VP6, and VP7) and six nonstructural proteins (NSP1 to NSP6) (2). RVs are classified into 8 species (A to H) by the antigenicity of the VP6 protein (3). Group A rotavirus (RVA) is a major cause of human RV-associated gastroenteritis (4). RVA can be classified into various G and P types on the basis of glycoprotein VP7 and protease-sensitive VP4, respectively. To date, at least 27 G and 35 P genotypes have been reported (5). The fact that the segmented genome undergoes point mutations, reassortment, and gene rearrangements accounts for the large genetic diversity of RVs (1).VP4 can be cleaved by protease to yield N-terminal VP8* and C-terminal VP5* (6). VP8* includes the VP4 spike head and is reported to bind to cell surface glycans essential for cell invasion (7). The ability of a virus to invade host cells is crucial for its replication, host tropism, and pathogenicity. Notably, VP8* is the most variable domain. VP8* proteins of sialidase-sensitive RVs were reported to interact with sialic acids (Sia) (8); however, most animal RVs and almost all human RVs were sialidase insensitive (9). It was noted that many of the sialidase-insensitive RVA strains interact with Sia at subterminal sites of glycoprotein receptors (10). Recently, histo-blood group antigens (HBGAs) have been reported to be attachment factors for human RVs by interacting with VP8* (11,12). HBGAs are a group of carbohydrates present on the surfaces of red blood cells and mucosal epithelia and as free oligosaccharides in saliva, blood, and milk (13).Previous studies by oligosaccharide and saliva binding assays showed that P

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“…P [19] is a rare RVA P genotype reported in humans and pigs (4). It was found to be combined with various G genotypes (23).…”

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Functional and Structural Characterization of P[19] Rotavirus VP8* Interaction with Histo-blood Group Antigens

Sun

Peng

et al. 2016

J Virol

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Epidemiologic Association BetweenFUT2Secretor Status and Severe Rotavirus Gastroenteritis in Children in the United States

et al. 2015

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IMPORTANCE A genetic polymorphism affecting FUT2 secretor status in approximately one-quarter of humans of European descent affects the expression of histo-blood group antigens on the mucosal epithelia of human respiratory, genitourinary, and digestive tracts. These histo-blood group antigens serve as host receptor sites necessary for attachment and infection of some pathogens, including norovirus.OBJECTIVE We investigated whether an association exists between FUT2 secretor status and laboratory-confirmed rotavirus infections in US children. DESIGN, SETTING, AND PARTICIPANTSMulticenter case-control observational study involving active surveillance at 6 US pediatric medical institutions in the inpatient and emergency department clinical settings. We enrolled 1564 children younger than 5 years with acute gastroenteritis (diarrhea and/or vomiting) and 818 healthy controls frequency matched by age and month, from December 1, 2011, through March 31, 2013. MAIN OUTCOMES AND MEASURESPaired fecal-saliva specimens were tested for rotavirus and for secretor status. Comparisons were made between rotavirus test-positive cases and healthy controls stratified by ethnicity and vaccination status. Adjusted multivariable analyses assessed the preventive association of secretor status against severe rotavirus gastroenteritis.RESULTS One (0.5%) of 189 rotavirus test-positive cases was a nonsecretor, compared with 188 (23%) of 818 healthy control participants (P < .001). Healthy control participants of Hispanic ethnicity were significantly less likely to be nonsecretors (13%) compared with healthy children who were not of Hispanic ethnicity (25%) (P < .001). After controlling for vaccination and other factors, children with the nonsecretor FUT2 polymorphism appeared statistically protected (98% [95% CI, 84%-100%]) against severe rotavirus gastroenteritis. CONCLUSIONS AND RELEVANCESevere rotavirus gastroenteritis was virtually absent among US children who had a genetic polymorphism that inactivates FUT2 expression on the intestinal epithelium. We observed a strong epidemiologic association among children with rotavirus gastroenteritis compared with healthy control participants. The exact cellular mechanism behind this epidemiologic association remains unclear, but evidence suggests that it may be rotavirus genotype specific. The lower prevalence of nonsecretors among Hispanic children may translate to an enhanced burden of rotavirus gastroenteritis among this group. Our findings may have bearing on our full understanding of rotavirus infections and the effects of vaccination in diverse populations.

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Substantial Receptor‐induced Structural Rearrangement of Rotavirus VP8*: Potential Implications for Cross‐Species Infection

Mishra

Holloway

et al. 2015

ChemBioChem

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Rotavirus-cell binding is the essential first step in rotavirus infection. This binding is a major determinant of rotavirus tropism, as host cell invasion is necessary to initiate infection. Initial rotavirus-cell interactions are mediated by carbohydrate-recognizing domain VP8* of the rotavirus capsid spike protein VP4. Here, we report the first observation of significant structural rearrangement of VP8* from human and animal rotavirus strains upon glycan receptor binding. The structural adaptability of rotavirus VP8* delivers important insights into how human and animal rotaviruses utilize the wider range of cellular glycans identified as VP8* binding partners. Furthermore, our studies on rotaviruses with atypical genetic makeup provide information expected to be critical for understanding the mechanisms of animal rotavirus gene emergence in humans and support implementation of epidemiologic surveillance of animal reservoirs as well as future vaccination schemes.

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Revisiting the role of histo-blood group antigens in rotavirus host-cell invasion

Abstract: Histo-blood group antigens (HBGAs)

Cited by 80 publications

References 69 publications

Functional and Structural Characterization of P[19] Rotavirus VP8* Interaction with Histo-blood Group Antigens

Functional and Structural Characterization of P[19] Rotavirus VP8* Interaction with Histo-blood Group Antigens

Epidemiologic Association BetweenFUT2Secretor Status and Severe Rotavirus Gastroenteritis in Children in the United States

Substantial Receptor‐induced Structural Rearrangement of Rotavirus VP8*: Potential Implications for Cross‐Species Infection

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