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. 2020 Dec 22;9:e58242. doi: 10.7554/eLife.58242

Figure 1. Composition and neutralization potency of recombinantly-derived bank vole mAb P-4G2.

(A) Composition of the complementarity-determining regions (CDRs) of the mAb P-4G2 antigen-binding fragment (Fab) heavy (VH) and kappa (VK) chains. For the full sequence of Fab P-4G2 variable regions, please see Figure 1—figure supplement 1. (B) A hantavirus-pseudotyped VSV-ΔG RFP neutralization assay shows that recombinantly produced mAb P-4G2 neutralizes Puumala virus- and Andes virus-pseudotyped VSV (black and blue traces, respectively), but not Hantaan virus-pseudotyped VSV (gray trace). Each neutralization assay was carried out three times in duplicate. A representative experiment is shown. Error bars represent the range of the value for the experiment performed in duplicate.

Figure 1.

Figure 1—figure supplement 1. Sequence alignment of antibody variable regions from bank vole mAb P-4G2 and a representative mouse antibody.

Figure 1—figure supplement 1.

Fab P-4G2 variable regions with variable regions from representative mouse (Mus musculus) antibodies. Mouse homologues used in the alignment were identified by NCBI BLAST (Altschul et al., 1990; Johnson et al., 2008). The P-4G2 heavy chain variable region (VH) was aligned with the VH sequence from mouse IgG (GenBank: BAN14007.1). The P-4G2 light chain variable region (VK) was aligned with the VK sequence from mouse IgG (GenBank: ATI98427.1). Complementarity-determining regions (CDRs) of P-4G2 are annotated under the alignment.