MDCK-B4GalNT2 cells disclose a α2,3-sialic acid requirement for the 2009 pandemic H1N1 A/California/04/2009 and NA aid entry of A/WSN/33

References

• Rogers GN, Paulson JC. Receptor determinants of human and animal influenza virus isolates: differences in receptor specificity of the H3 hemagglutinin based on species of origin. Virology. 1983;127(2):361–373. doi: 10.1016/0042-6822(83)90150-2
   PubMed Web of Science ®Google Scholar
• Rogers GN, Dsouza BL. Receptor binding properties of human and animal H1 influenza virus isolates. Virology. 1989 Nov;173(1):317–322. doi: 10.1016/0042-6822(89)90249-3
   PubMed Web of Science ®Google Scholar
• Nicholls JM, Bourne AJ, Chen H, et al. Sialic acid receptor detection in the human respiratory tract: evidence for widespread distribution of potential binding sites for human and avian influenza viruses. Respir Res. 2007;8(1):73. doi: 10.1186/1465-9921-8-73
   PubMed Web of Science ®Google Scholar
• Walther T, Karamanska R, Chan RWY, et al. Glycomic analysis of human respiratory tract tissues and correlation with influenza virus infection. PLoS Pathog. 2013;9(3):e1003223. doi: 10.1371/journal.ppat.1003223
   PubMed Web of Science ®Google Scholar
• Costa T, Chaves AJ, Valle R, et al. Distribution patterns of influenza virus receptors and viral attachment patterns in the respiratory and intestinal tracts of seven avian species. Vet Res. 2012;43(1):28. doi: 10.1186/1297-9716-43-28
   PubMed Web of Science ®Google Scholar
• Gulati S, Smith DF, Cummings RD, et al. Human H3N2 influenza viruses isolated from 1968 to 2012 show varying preference for receptor substructures with no apparent consequences for disease or spread. PloS One. 2013;8(6):e66325. doi: 10.1371/journal.pone.0066325
   PubMed Web of Science ®Google Scholar
• Lin YP, Gregory V, Collins P, et al. Neuraminidase receptor binding variants of human influenza A (H3N2) viruses resulting from substitution of aspartic acid 151 in the catalytic site: a role in virus attachment? J Virol. 2010;84(13):6769–6781. doi: 10.1128/JVI.00458-10
   PubMed Web of Science ®Google Scholar
• Zhu X, McBride R, Nycholat CM, et al. Influenza virus neuraminidases with reduced enzymatic activity that avidly bind sialic acid receptors. J Virol. 2012;86(24):13371–13383. doi: 10.1128/JVI.01426-12
   PubMed Web of Science ®Google Scholar
• Hooper KA, Bloom JD. A mutant influenza virus that uses an N1 neuraminidase as the receptor-binding protein. J Virol. 2013;JVI:01889–01813.
   Google Scholar
• Hooper KA, Crowe JE, Bloom JD. Influenza viruses with receptor-binding N1 neuraminidases occur sporadically in several lineages and show no attenuation in cell culture or mice. J Virol. 2015;JVI:00012–00015.
   Google Scholar
• Guo H, Rabouw H, Slomp A, et al. Kinetic analysis of the influenza A virus HA/NA balance reveals contribution of NA to virus-receptor binding and NA-dependent rolling on receptor-containing surfaces. PLoS Pathog. 2018;14(8):e1007233. doi: 10.1371/journal.ppat.1007233
   PubMed Web of Science ®Google Scholar
• Lai JCC, Karunarathna HMTK, Wong HH, et al. Neuraminidase activity and specificity of influenza A virus are influenced by haemagglutinin-receptor binding. Emerg Microbes Infect. 2019;8(1):327–338. doi: 10.1080/22221751.2019.1581034
   PubMed Web of Science ®Google Scholar
• Leigh MW, Connor RJ, Kelm S, et al. Receptor specificity of influenza virus influences severity of illness in ferrets. Vaccine. 1995;13(15):1468–1473. doi: 10.1016/0264-410X(95)00004-K
   PubMed Web of Science ®Google Scholar
• Kirkeby S, Martel CJM, Aasted B. Infection with human H1N1 influenza virus affects the expression of sialic acids of metaplastic mucous cells in the ferret airways. Virus Res. 2009;144(1):225–232. doi: 10.1016/j.virusres.2009.05.004
   PubMed Web of Science ®Google Scholar
• Jia N, Barclay WS, Roberts K, et al. Glycomic characterization of respiratory tract tissues of ferrets implications for its use in influenza virus infection studies. J Biol Chem. 2014 Oct;289(41):28489–28504. doi: 10.1074/jbc.M114.588541
   PubMed Web of Science ®Google Scholar
• Dall'Olio F, Malagolini N, Chiricolo M, et al. The expanding roles of the Sda/Cad carbohydrate antigen and its cognate glycosyltransferase B4GALNT2. Biochim Biophys Acta. 2014;1840(1):443–453. doi: 10.1016/j.bbagen.2013.09.036
   PubMed Web of Science ®Google Scholar
• Morton J, Pickles M, Terry A. The SdaBlood group antigen in tissues and body fluids. Vox Sang. 1970;19(5-6):472–482.
   PubMed Web of Science ®Google Scholar
• Groux-Degroote S, Wavelet C, Krzewinski-Recchi M-A, et al. B4GALNT2 gene expression controls the biosynthesis of Sd a and sialyl Lewis X antigens in healthy and cancer human gastrointestinal tract. Int J Biochem Cell Biol. 2014;53:442–449. doi: 10.1016/j.biocel.2014.06.009
   PubMed Web of Science ®Google Scholar
• Kohl KD, Oakeson KF, Dunn D, et al. Patterns of host gene expression associated with harboring a foregut microbial community. BMC Genomics. 2017;18(1):697. doi: 10.1186/s12864-017-4101-z
   PubMed Web of Science ®Google Scholar
• Staubach F, Künzel S, Baines AC, et al. Expression of the blood-group-related glycosyltransferase B4galnt2 influences the intestinal microbiota in mice. ISME J. 2012;6(7):1345–1355. doi: 10.1038/ismej.2011.204
   PubMed Web of Science ®Google Scholar
• Hooper LV, Gordon JI. Glycans as legislators of host–microbial interactions: spanning the spectrum from symbiosis to pathogenicity. Glycobiology. 2001;11(2):1R–10R. doi: 10.1093/glycob/11.2.1R
   PubMed Web of Science ®Google Scholar
• Rausch P, Steck N, Suwandi A, et al. Expression of the blood-group-related gene B4galnt2 alters susceptibility to Salmonella infection. PLoS Pathog. 2015;11(7):e1005008. doi: 10.1371/journal.ppat.1005008
   PubMed Web of Science ®Google Scholar
• Malagolini N, Santini D, Chiricolo M, et al. Biosynthesis and expression of the Sda and sialyl Lewis x antigens in normal and cancer colon. Glycobiology. 2007;17(7):688–697. doi: 10.1093/glycob/cwm040
   PubMed Web of Science ®Google Scholar
• Kawamura Y, Adachi Y, Curiel D, et al. Therapeutic adenoviral gene transfer of a glycosyltransferase for prevention of peritoneal dissemination and metastasis of gastric cancer. Cancer Gene Ther. 2014;21(10):427. doi: 10.1038/cgt.2014.46
   PubMed Web of Science ®Google Scholar
• Kawamura YI, Toyota M, Kawashima R, et al. DNA hypermethylation contributes to incomplete synthesis of carbohydrate determinants in gastrointestinal cancer. Gastroenterology. 2008;135(1):142–151.e3. doi: 10.1053/j.gastro.2008.03.031
   PubMed Web of Science ®Google Scholar
• Byrne GW, McGregor CG, Breimer ME. Recent investigations into pig antigen and anti-pig antibody expression. Int J Surg. 2015;23:223–228. doi: 10.1016/j.ijsu.2015.07.724
   PubMed Web of Science ®Google Scholar
• Wang Z-Y, Li P, Butler JR, et al. Immunogenicity of renal microvascular endothelial cells from genetically modified pigs. Transplantation. 2016;100(3):533–537. doi: 10.1097/TP.0000000000001070
   PubMed Web of Science ®Google Scholar
• Heaton BE, Kennedy EM, Dumm RE, et al. A CRISPR activation screen identifies a pan-avian influenza virus inhibitory host factor. Cell Rep. 2017;20(7):1503–1512. doi: 10.1016/j.celrep.2017.07.060
   PubMed Web of Science ®Google Scholar
• Hoffmann E, Neumann G, Kawaoka Y, et al. A DNA transfection system for generation of influenza A virus from eight plasmids. Proc Natl Acad Sci U S A. 2000;97(11):6108–6113. doi: 10.1073/pnas.100133697
   PubMed Web of Science ®Google Scholar
• Chin AW, Leong NK, Nicholls JM, et al. Characterization of influenza A viruses with polymorphism in PB2 residues 701 and 702. Sci Rep. 2017;7(1):11361. doi: 10.1038/s41598-017-11625-y
   PubMed Web of Science ®Google Scholar
• Sakai T, Ohuchi M, Imai M, et al. Dual wavelength imaging allows analysis of membrane fusion of influenza virus inside cells. J Virol. 2006;80(4):2013–2018. doi: 10.1128/JVI.80.4.2013-2018.2006
   PubMed Web of Science ®Google Scholar
• Lee J, Kim J, Son K, et al. Acid phosphatase 2 (ACP2) is required for membrane fusion during influenza virus entry. Sci Rep. 2017;7:1–13. doi: 10.1038/s41598-016-0028-x
   PubMed Web of Science ®Google Scholar
• Matrosovich M, Matrosovich T, Carr J, et al. Overexpression of the α-2, 6-sialyltransferase in MDCK cells increases influenza virus sensitivity to neuraminidase inhibitors. J Virol. 2003;77(15):8418–8425. doi: 10.1128/JVI.77.15.8418-8425.2003
   PubMed Web of Science ®Google Scholar
• Wu C-Y, Lin C-W, Tsai T-I, et al. Influenza A surface glycosylation and vaccine design. Proc Natl Acad Sci U S A. 2017;114(2):280–285. doi: 10.1073/pnas.1617174114
   PubMed Web of Science ®Google Scholar
• Leung HS, Li OT, Chan RW, et al. The virus entry of influenza A virus with a α2, 6-linked sialic acid binding preference requires host fibronectin. J Virol. 2012;JVI:01166–01112.
   Google Scholar
• Bradley KC, Jones CA, Tompkins SM, et al. Comparison of the receptor binding properties of contemporary swine isolates and early human pandemic H1N1 isolates (Novel 2009 H1N1). Virology. 2011;413(2):169–182. doi: 10.1016/j.virol.2011.01.027
   PubMed Web of Science ®Google Scholar
• Chen L-M, Rivailler P, Hossain J, et al. Receptor specificity of subtype H1 influenza A viruses isolated from swine and humans in the United States. Virology. 2011;412(2):401–410. doi: 10.1016/j.virol.2011.01.015
   PubMed Web of Science ®Google Scholar
• Maines TR, Jayaraman A, Belser JA, et al. Transmission and pathogenesis of swine-origin 2009 A (H1N1) influenza viruses in ferrets and mice. Science. 2009;325(5939):484–487. doi: 10.1126/science.1177238
   PubMed Web of Science ®Google Scholar
• Yang H, Carney P, Stevens J. Structure and receptor binding properties of a pandemic H1N1 virus hemagglutinin. PLoS Curr. 2010;2:1–17. doi: 10.1371/currents.RRN1152
   Google Scholar
• Soundararajan V, Tharakaraman K, Raman R, et al. Extrapolating from sequence—the 2009 H1N1 ‘swine’ influenza virus. Nat Biotechnol. 2009;27(6):510–513. doi: 10.1038/nbt0609-510
   PubMed Web of Science ®Google Scholar
• Childs RA, Palma AS, Wharton S, et al. Receptor-binding specificity of pandemic influenza A (H1N1) 2009 virus determined by carbohydrate microarray. Nat Biotechnol. 2009;27(9):797–799. doi: 10.1038/nbt0909-797
   PubMed Web of Science ®Google Scholar
• Xu R, McBride R, Nycholat CM, et al. Structural characterization of the hemagglutinin receptor specificity from the 2009 H1N1 influenza pandemic. J Virol. 2012;86(2):982–990. doi: 10.1128/JVI.06322-11
   PubMed Web of Science ®Google Scholar
• Mayr J, Lau K, Lai JC, et al. Unravelling the role of O-glycans in influenza A virus infection. Sci Rep. 2018;8(1):16382. doi: 10.1038/s41598-018-34175-3
   PubMed Web of Science ®Google Scholar