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Structural Basis for Cell Wall Recognition by Bacteriophage PBC5 Endolysin

42 Pages Posted: 24 Dec 2018 Publication Status: Published

See all articles by Ko On Lee

Ko On Lee

Seoul National University - Department of Agricultural Biotechnology; Seoul National University - Research Institute of Agriculture and Life Sciences; Korea Basic Science Institute - Protein Structure Research Team

Minsuk Kong

Seoul National University - Department of Agricultural Biotechnology; Seoul National University - Research Institute of Agriculture and Life Sciences

Jaewoo Bai

Seoul National University - Department of Agricultural Biotechnology; Seoul National University - Research Institute of Agriculture and Life Sciences

Soyoung Cha

Korea Basic Science Institute - Protein Structure Research Team

Iktae Kim

Seoul National University - Department of Agricultural Biotechnology; Seoul National University - Research Institute of Agriculture and Life Sciences

Kyoung-Seok Ryu

Korea Basic Science Institute - Protein Structure Research Team

Sangryeol Ryu

Seoul National University - Department of Agricultural Biotechnology; Seoul National University - Research Institute of Agriculture and Life Sciences

Jeong-Yong Suh

Seoul National University - Department of Agricultural Biotechnology; Seoul National University - Research Institute of Agriculture and Life Sciences; Shinshu University - Institute for Biomedical Sciences

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Abstract

Phage endolysins are hydrolytic enzymes that cleave the bacterial cell wall during the lytic cycle. We isolated the bacteriophage PBC5 against Bacillus cereus, 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 structure of CBD reveals tandem SH3b domains that are tightly engaged with each other. CBD binds to peptidoglycan in a bidentate manner via distal β-sheet motifs with pseudo two-fold symmetry, which can explain its high affinity and host specificity. 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.

Suggested Citation

Lee, Ko On and Kong, Minsuk and Bai, Jaewoo and Cha, Soyoung and Kim, Iktae and Ryu, Kyoung-Seok and Ryu, Sangryeol and Suh, Jeong-Yong, Structural Basis for Cell Wall Recognition by Bacteriophage PBC5 Endolysin (December 22, 2018). Available at SSRN: https://ssrn.com/abstract=3305589 or http://dx.doi.org/10.2139/ssrn.3305589
This version of the paper has not been formally peer reviewed.

Ko On Lee

Seoul National University - Department of Agricultural Biotechnology

Seoul
Korea, Republic of (South Korea)

Seoul National University - Research Institute of Agriculture and Life Sciences

Seoul
Korea, Republic of (South Korea)

Korea Basic Science Institute - Protein Structure Research Team

162 Yeongudanji-Ro
Ochang-Eup, Cheongju-Si
Chungcheongbuk-Do, 28119
Korea, Republic of (South Korea)

Minsuk Kong

Seoul National University - Department of Agricultural Biotechnology

Seoul
Korea, Republic of (South Korea)

Seoul National University - Research Institute of Agriculture and Life Sciences

Seoul
Korea, Republic of (South Korea)

Jaewoo Bai

Seoul National University - Department of Agricultural Biotechnology

Seoul
Korea, Republic of (South Korea)

Seoul National University - Research Institute of Agriculture and Life Sciences

Seoul
Korea, Republic of (South Korea)

Soyoung Cha

Korea Basic Science Institute - Protein Structure Research Team

162 Yeongudanji-Ro
Ochang-Eup, Cheongju-Si
Chungcheongbuk-Do, 28119
Korea, Republic of (South Korea)

Iktae Kim

Seoul National University - Department of Agricultural Biotechnology

Seoul
Korea, Republic of (South Korea)

Seoul National University - Research Institute of Agriculture and Life Sciences

Seoul
Korea, Republic of (South Korea)

Kyoung-Seok Ryu

Korea Basic Science Institute - Protein Structure Research Team

162 Yeongudanji-Ro
Ochang-Eup, Cheongju-Si
Chungcheongbuk-Do, 28119
Korea, Republic of (South Korea)

Sangryeol Ryu

Seoul National University - Department of Agricultural Biotechnology

Seoul
Korea, Republic of (South Korea)

Seoul National University - Research Institute of Agriculture and Life Sciences

Seoul
Korea, Republic of (South Korea)

Jeong-Yong Suh (Contact Author)

Seoul National University - Department of Agricultural Biotechnology ( email )

Seoul
Korea, Republic of (South Korea)

Seoul National University - Research Institute of Agriculture and Life Sciences ( email )

Seoul
Korea, Republic of (South Korea)

Shinshu University - Institute for Biomedical Sciences ( email )

Minamiminowa
Nagano, 399-4598
Japan