Fig. 3

Alignment and electrostatic surface potential analysis of key amino acids residues of NRP1. A Sequence alignment analysis of the interface binding between NRP1 and S of SARS-CoV-2 from humans (GenBank accession no. XP_006717584.1), rhesus monkeys (GenBank accession no. NP_001252745.1), ferrets (GenBank accession no. XP_004774343.2), minks (GenBank accession no. XP_044082878.1), bovines (GenBank accession no. NP_001192589.1), hamsters (GenBank accession no. XP_007647231.1), and mice (GenBank accession no. XP_0065430829.1). The NRP1 residues at positions 35 and 90 are marked with blue triangles. B Electrostatic surface potential diagram of ACE2s in different species. The structural superposition of the NRP1 region 28–140 from cattle (green), minks (brown), ferrets (cyan), mice (gray), hamsters (pink), humans (khaki), and rhesus monkeys (blue) is in the center. The homology models of human NRP1 (PDBID 7m0r) were used to compare the NRP1 structures of cattle, minks, ferrets, mice, hamsters, and rhesus monkeys. The tertiary structure was predicted using SWISS-MODEL. The yellow sticks highlight the two key differential resides of NRP1 binding with S of SARS-CoV-2. The details are circled using a dashed line in each electrostatic surface potential map. The electrostatic potential color range is –/ + 5