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Lectins enhance SARS-CoV-2 infection and influence neutralizing antibodies

机译：凝集素增强SARS-COV-2感染和影响中和抗体

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SARS-CoV-2 infection-which involves both cell attachment and membrane fusion-relies on the angiotensin-converting enzyme 2 (ACE2) receptor, which is paradoxically found at low levels in the respiratory tract(1-3), suggesting that there may be additional mechanisms facilitating infection. Here we show that C-type lectin receptors, DC-SIGN, L-SIGN and the sialic acid-binding immunoglobulin-like lectin 1 (SIGLEC1) function as attachment receptors by enhancing ACE2-mediated infection and modulating the neutralizing activity of different classes of spike-specific antibodies. Antibodies to the amino-terminal domain or to the conserved site at the base of the receptor-binding domain, while poorly neutralizing infection of ACE2-overexpressing cells, effectively block lectin-facilitated infection. Conversely, antibodies to the receptor binding motif, while potently neutralizing infection of ACE2-overexpressing cells, poorly neutralize infection of cells expressing DC-SIGN or L-SIGN and trigger fusogenic rearrangement of the spike, promoting cell-to-cell fusion. Collectively, these findings identify a lectin-dependent pathway that enhances ACE2-dependent infection by SARS-CoV-2 and reveal distinct mechanisms of neutralization by different classes of spike-specific antibodies.
机译：SARS-COV-2感染 - 涉及细胞连接和膜融合 - 依赖于血管紧张素转换酶2（ACE2）受体，其在呼吸道（1-3）的低水平下矛盾地发现，表明可能存在是促进感染的额外机制。在这里，我们通过增强ACE2介导的感染并调节不同类别的中和活性来表明C型凝集素受体，DC-符号，L-符号和唾液酸结合免疫球蛋白样凝集素1（SigleC1）用作附着受体，并调节不同类别的中和活性穗状状抗体。氨基 - 末端结构域的抗体或受体结合结构域碱的保守部位，同时有效地阻断凝集素促进感染的αce2-过表达细胞的感染差。相反，对受体结合基序的抗体，同时对ACE2过表达细胞的易感性感染，表达DC标志或L标志的细胞感染不良，并引发尖峰的致密性重排，促进细胞对细胞融合。总的来说，这些发现鉴定了依赖依赖性衔接途径，其增强了SARS-COV-2的ACE2依赖性感染，并揭示了不同类别的穗状特异性抗体中和的明显的中和机制。

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