Id |
Subject |
Object |
Predicate |
Lexical cue |
T328 |
0-103 |
Sentence |
denotes |
In α-CoVs such as TGEV, HA-activity is attributed to the SA-recognizing activity to α2,3-NeuGc [61,62]. |
T329 |
104-190 |
Sentence |
denotes |
The SA-binding site is present on the N-terminal region of the S-glycoprotein of TGEV. |
T330 |
191-247 |
Sentence |
denotes |
TGEV has two types with enteric and respiratory tropism. |
T331 |
248-346 |
Sentence |
denotes |
The respiratory TGEV has the porcine aminopeptidase N (pAPN)-binding domain and SA-binding domain. |
T332 |
347-503 |
Sentence |
denotes |
Nucleotide 655 of the S gene is essential for enteric tropism and the S219A mutation of the S glycoprotein confers the enteric to respiratory tropism shift. |
T333 |
504-672 |
Sentence |
denotes |
In addition, a 6-nucleotide insertional mutation at nucleotide 1124, which yields the Y374-T375insND shift of the S glycoprotein, causes enhanced enteric tract tropism. |
T334 |
673-832 |
Sentence |
denotes |
TGEV interacts with SA species on mucin-like glycoprotein (MGP), a highly glycosylated protein, in an SA-dependent manner, on mucin-secreting goblet cells [6]. |
T335 |
833-917 |
Sentence |
denotes |
MGP SA-binding allows virus entry via the mucus layer to the intestinal enterocytes. |
T336 |
918-1072 |
Sentence |
denotes |
Different from TGEV, the S glycoprotein of porcine CoV has no hemagglutination activity due to deletion of the SA-binding site of the S glycoprotein [61]. |
T337 |
1073-1150 |
Sentence |
denotes |
The loss of SA-binding activity is correlated to the non-enteropathogenicity. |
T338 |
1151-1340 |
Sentence |
denotes |
SAs function as HA-mediated entry determinants for TGEV, causing the enteropathogenic outcome of the virus, and SA-recognition activity is also responsible for virus amplification in cells. |
T339 |
1341-1450 |
Sentence |
denotes |
SA-binding activity-deficient TGEV can propagate in cells through pAPN, known as CD13, as a receptor [62,63]. |
T340 |
1451-1537 |
Sentence |
denotes |
The SA-binding activity potentiates infection and is crucial for intestinal infection. |