Structural Basis for Cell-Wall Recognition by Bacteriophage PBC5 Endolysin

다국어 초록 (Multilingual Abstract)

<P><B>Summary</B></P> <P>Phage endolysins are hydrolytic enzymes that cleave the bacterial cell wall during the lytic cycle. We isolated the bacteriophage PBC5 against <I>Bacillus cereus</I>, a major foodborne pathogen, and describe the molecular interaction between endolysin LysPBC5 and the host peptidoglycan structure. LysPBC5 has an N-terminal glycoside hydrolase 25 domain, and a C-terminal cell-wall binding domain (CBD) that is critical for specific cell-wall recognition and lysis. The crystal and solution structures of CBDs reveal tandem SH3b domains that are tightly engaged with each other. The CBD binds to the peptidoglycan in a bidentate manner via distal β sheet motifs with pseudo 2-fold symmetry, which can explain its high affinity and host specificity. The CBD primarily interacts with the glycan strand of the peptidoglycan layer instead of the peptide crosslink, implicating the tertiary structure of peptidoglycan as the recognition motif of endolysins.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Phage PBC5 encodes a novel endolysin LysPBC5 against <I>Bacillus cereus</I> </LI> <LI> LysPBC5 recognizes host cell walls via a conjoined tandem SH3b repeat fold </LI> <LI> The SH3b repeat fold interacts with peptidoglycans in a bidentate manner </LI> <LI> LysPBC5 primarily binds to glycan strands of the cell-wall structure </LI> </UL> </P> <P><B>Graphical Abstract</B></P> <P>[DISPLAY OMISSION]</P>