PLoS Pathog . Significant role of host sialylated glycans in the infection and spread of severe acute respiratory syndrome coronavirus 2

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PLoS Pathog


. 2022 Jun 14;18(6):e1010590.
doi: 10.1371/journal.ppat.1010590. eCollection 2022 Jun.
Significant role of host sialylated glycans in the infection and spread of severe acute respiratory syndrome coronavirus 2


Wakana Saso ^{1 2 3} , Masako Yamasaki ^{1 4} , Shin-Ichi Nakakita ⁵ , Shuetsu Fukushi ⁶ , Kana Tsuchimoto ⁷ , Noriyuki Watanabe ¹ , Nongluk Sriwilaijaroen ^{8 9} , Osamu Kanie ¹⁰ , Masamichi Muramatsu ¹ , Yoshimasa Takahashi ⁷ , Tetsuro Matano ^{2 3} , Makoto Takeda ¹¹ , Yasuo Suzuki ⁹ , Koichi Watashi ^{1 4 7 12 13}



Affiliations

• PMID: 35700214
• DOI: 10.1371/journal.ppat.1010590

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been transmitted across all over the world, in contrast to the limited epidemic of genetically- and virologically-related SARS-CoV. However, the molecular basis explaining the difference in the virological characteristics among SARS-CoV-2 and SARS-CoV has been poorly defined. Here we identified that host sialoglycans play a significant role in the efficient spread of SARS-CoV-2 infection, while this was not the case with SARS-CoV. SARS-CoV-2 infection was significantly inhibited by α2-6-linked sialic acid-containing compounds, but not by α2-3 analog, in VeroE6/TMPRSS2 cells. The α2-6-linked compound bound to SARS-CoV-2 spike S1 subunit to competitively inhibit SARS-CoV-2 attachment to cells. Enzymatic removal of cell surface sialic acids impaired the interaction between SARS-CoV-2 spike and angiotensin-converting enzyme 2 (ACE2), and suppressed the efficient spread of SARS-CoV-2 infection over time, in contrast to its least effect on SARS-CoV spread. Our study provides a novel molecular basis of SARS-CoV-2 infection which illustrates the distinctive characteristics from SARS-CoV.