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. 2023 Jul 18;12:e86369. doi: 10.7554/eLife.86369

Figure 1. Sequence alignment and analysis of orthologous proteins to human bactericidal/permeability-increasing protein (huBPI).

(A) Sequence alignment of amino acid sequences of orthologous proteins. Functional regions I–III are framed, and positively charged amino acids are shown in blue. The amino acid sequence mediating the bactericidal activity of human BPI (huBPI) is underlined. (B) Functional regions I–III (dark grey) as shown for huBPI. (C) Phylogenetic tree analysis mapping BPI orthologous proteins to their respective taxonomic ranks. (D) Number of basic amino acids in regions I–III as shown for oyster BPI (osBPI), scorpionfish BPI (scoBPI), huBPI and murine BPI (muBPI). (E) Electrostatic surface potentials calculated for the N-terminal barrel of osBPI, scoBPI, huBPI, and muBPI. Negatively charged areas are colored in red, and positively charged domains are shown in blue.

Figure 1.

Figure 1—figure supplement 1. Sequence alignment and analysis of orthologous Actinopterygii bactericidal/permeability-increasing protein (BPI).

Figure 1—figure supplement 1.

(A) Sequence alignment of amino acid sequences of orthologous proteins.Functional regions I–III are framed, and positively charged amino acids are shown in blue. Conserved areas are indicated by asterisk, colon and period representing highly, moderately, and less conserved areas, respectively. (B) Number of basic amino acids in regions I–III of Actinopterygii BPI. (C) Actinopterygii species are listed including taxonomic family, abbreviation of the corresponding BPI and UniProt ID. (D) Phylogenetic tree analysis mapping Actinopterygii BPI orthologous to their respective taxonomic ranks.
Figure 1—figure supplement 2. Predicted N-terminal surface electrostatics and sequence identities of Actinopterygii bactericidal/permeability-increasing protein (BPI).

Figure 1—figure supplement 2.

(A) Surface electrostatics for the N-terminal barrels of three-dimensional structure predictions for BPI of investigated Actinopterygii. Areas colored in blue represent positively charged areas, and negatively charged domains are shown in red. (B) Sequence identities of investigated orthologous proteins without signal peptide in comparison to scorpionfish BPI (scoBPI) and human BPI (huBPI).
Figure 1—figure supplement 2—source data 1. Uncropped and labeled images for Figure 2—figure supplement 1C.
Raw data for Figure 2—figure supplement 1D.