The SARS-CoV-2 Lambda variant exhibits enhanced infectivity and immune resistance

Izumi Kimura, Yusuke Kosugi, Jiaqi Wu, Jiri Zahradnik, Daichi Yamasoba, Erika P Butlertanaka, Yuri L Tanaka, Keiya Uriu, Yafei Liu, Nanami Morizako, Kotaro Shirakawa, Yasuhiro Kazuma, Ryosuke Nomura, Yoshihito Horisawa, Kenzo Tokunaga, Takamasa Ueno, Akifumi Takaori-Kondo, Gideon Schreiber, Hisashi Arase, Akatsuki SaitoChihiro Motozono, So Nakagawa, Kei Sato

Research output: Contribution to journalArticlepeer-review


SARS-CoV-2 Lambda, a variant of interest, has spread in some South American countries; however, its virological features and evolutionary traits remain unclear. In this study, we use pseudoviruses and reveal that the spike protein of the Lambda variant is more infectious than that of other variants due to the T76I and L452Q mutations. The RSYLTPGD246-253N mutation, a unique 7-amino acid deletion in the N-terminal domain of the Lambda spike protein, is responsible for evasion from neutralizing antibodies and further augments antibody-mediated enhancement of infection. Although this mutation generates a nascent N-linked glycosylation site, the additional N-linked glycan is dispensable for the virological property conferred by this mutation. Since the Lambda variant has dominantly spread according to the increasing frequency of the isolates harboring the RSYLTPGD246-253N mutation, our data suggest that the RSYLTPGD246-253N mutation is closely associated with the substantial spread of the Lambda variant in South America.

Original languageEnglish
Article number110218
JournalCell Reports
Issue number2
StatePublished - 11 Jan 2022

All Science Journal Classification (ASJC) codes

  • General Biochemistry,Genetics and Molecular Biology


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