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In addition, both NoVs and RVs are highly diverse in how they recognise these HBGAs. Structural analysis of the HBGA-binding interfaces of NoVs revealed a conserved central binding pocket (CBP) interacting with a common major binding saccharide (MaBS) of HBGAs and a variable surrounding region interacting with additional minor binding saccharides. The conserved CBP indicates a strong selection of NoVs by the host HBGAs, whereas the variable surrounding region explains the diverse recognition patterns of different HBGAs by NoVs and RVs as functional adaptations of the viruses to human HBGAs. Diverse recognition of HBGAs has also been found in bacterial pathogen\n                    <jats:italic>Helicobacter pylori<\/jats:italic>\n                    . Thus, exploratory research into whether such diverse recognitions also occur for other viral and bacterial pathogens that recognise HBGAs is warranted.\n                  <\/jats:p>","DOI":"10.1017\/erm.2014.2","type":"journal-article","created":{"date-parts":[[2014,3,10]],"date-time":"2014-03-10T04:38:37Z","timestamp":1394426317000},"source":"Crossref","is-referenced-by-count":154,"title":["Histo-blood group antigens: a common niche for norovirus and rotavirus"],"prefix":"10.1017","volume":"16","author":[{"given":"Ming","family":"Tan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xi","family":"Jiang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"56","published-online":{"date-parts":[[2014,3,10]]},"reference":[{"key":"S1462399414000027_ref85","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2007.01.028"},{"key":"S1462399414000027_ref4","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1000983"},{"key":"S1462399414000027_ref83","unstructured":"(2011) Rotavirus surveillance \u2013 worldwide, 2009. 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