| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T228 |
0-510 |
Sentence |
denotes |
The genomes of new IAV subtypes, H17N10, which was identified in liver, intestine, lung and kidney tissues and in rectal swabs, but not in oral swabs, of frugivorous yellow-shouldered bats (Sturnira lilium, family Phyllostomidae) in Guatemala [119], and H18N11, which was identified in intestine tissue and in rectal swabs of frugivorous flat-faced bats (Artibeus planirostris, family Phyllostomidae) in Peru [120] during the period from 2009 to 2010, were reported in 2012 and in 2013, respectively (Table 1). |
| T229 |
511-693 |
Sentence |
denotes |
Based on aa sequences of H1–H18 HAs, both bat H17 and H18 HAs are more similar to H1–H2, H5–H6, H8–H9, H11–H13 and H16 in group 1 than to H3–H4, H7, H10 and H14–H15 in group 2 [198]. |
| T230 |
694-879 |
Sentence |
denotes |
Analysis of the crystal structures of bat H17 and H18 HAs revealed that their overall structures retain possession of typical IAV HA molecules including the receptor binding site (RBS). |
| T231 |
880-1049 |
Sentence |
denotes |
However, bat HAs showed no binding to any of 610 diverse structures of glycans including more than 100 sialylated glycans with either α2,3, α2,6, α2,8 or mixed linkages. |
| T232 |
1050-1709 |
Sentence |
denotes |
Detailed structural analysis (Figure 3d) revealed that at least four residues unique to bat H17 and H18 HAs seem to substantially reject a sialylated glycan from the bat RBS. (i) Highly conserved Y98 anchoring Sia is replaced by F98 in bat HAs. (ii) Highly conserved Q226 in H1 HAs and Q/L/I226 (a determinant of sialyl linkage specificity) in H3 HAs is replaced by H226 in bat HAs. (iii) The large residue D228 in bat HAs would make a steric clash with the side chain of Sia. (iv) The other large negatively charged residue D136 in bat HAs, possibly the most important residue, would provide electrostatic repulsion to a negatively charged sialylated glycan. |
| T233 |
1710-1844 |
Sentence |
denotes |
Both structural and functional studies on bat HAs strongly confirmed that bat H17 and H18 HAs do not bind to sialylated glycans [120]. |
