TY - JOUR
T1 - Screening and purification of NanB sialidase from Pasteurella multocida with activity in hydrolyzing sialic acid Neu5Acα(2–6)Gal and Neu5Acα(2–3)Gal
AU - Nugroho, Christian Marco Hadi
AU - Kurnia, Ryan Septa
AU - Tarigan, Simson
AU - Silaen, Otto Sahat Martua
AU - Triwidyaningtyas, Silvia
AU - Wibawan, I. Wayan Teguh
AU - Natalia, Lily
AU - Takdir, Andi Khomeini
AU - Soebandrio, Amin
N1 - Funding Information:
The author appreciates the help of Dr. Sudarisman and Drh. Adin Priadi (PT Medika Satwa Laboratories, Bogor-Indonesia) for their assistance and Microbiology Laboratory facilities. This study was funded by Universitas Indonesia through PUTI Grant with contract number NKB-1291/UN2.RST/HKP.05.00/2020.
Funding Information:
The author appreciates the help of Dr. Sudarisman and Drh. Adin Priadi (PT Medika Satwa Laboratories, Bogor-Indonesia) for their assistance and Microbiology Laboratory facilities. This study was funded by Universitas Indonesia through PUTI Grant with contract number NKB-1291/UN2.RST/HKP.05.00/2020.
Funding Information:
This article was funded by Universitas Indonesia, PUTI Grant NKB-1291/UN2.RST/HKP.05.00/2020.
Publisher Copyright:
© 2022, The Author(s).
PY - 2022/12
Y1 - 2022/12
N2 - Study on sialidases as antiviral agents has been widely performed, but many types of sialidase have not been tested for their antiviral activity. Pasteurella multocida NanB sialidase is one such sialidase that has never been isolated for further research. In this study, the activity of NanB sialidase was investigated in silico by docking the NanB sialidase of Pasteurella multocida to the Neu5Acα(2–6)Gal and Neu5Acα(2–3)Gal ligands. Additionally, some local isolates of Pasteurella multocida, which had the NanB gene were screened, and the proteins were isolated for further testing regarding their activity in hydrolyzing Neu5Acα(2–6)Gal and Neu5Acα(2–3)Gal. Silico studies showed that the NanB sialidase possesses an exceptional affinity towards forming a protein–ligand complex with Neu5Acα(2–6)Gal and Neu5Acα(2–3)Gal. NanB sialidase of Pasteurella multocida B018 at 0.129 U/mL and 0.258 U/mL doses can hydrolyze Neu5Acα(2–6)Gal and Neu5Acα(2–3)Gal better than other doses. In addition, those doses can inhibit effectively H9N2 viral binding to red blood cells. This study suggested that the NanB sialidase of Pasteurella multocida B018 has a potent antiviral activity because can hydrolyze sialic acid on red blood cells surface and inhibit the H9N2 viral binding to the cells.
AB - Study on sialidases as antiviral agents has been widely performed, but many types of sialidase have not been tested for their antiviral activity. Pasteurella multocida NanB sialidase is one such sialidase that has never been isolated for further research. In this study, the activity of NanB sialidase was investigated in silico by docking the NanB sialidase of Pasteurella multocida to the Neu5Acα(2–6)Gal and Neu5Acα(2–3)Gal ligands. Additionally, some local isolates of Pasteurella multocida, which had the NanB gene were screened, and the proteins were isolated for further testing regarding their activity in hydrolyzing Neu5Acα(2–6)Gal and Neu5Acα(2–3)Gal. Silico studies showed that the NanB sialidase possesses an exceptional affinity towards forming a protein–ligand complex with Neu5Acα(2–6)Gal and Neu5Acα(2–3)Gal. NanB sialidase of Pasteurella multocida B018 at 0.129 U/mL and 0.258 U/mL doses can hydrolyze Neu5Acα(2–6)Gal and Neu5Acα(2–3)Gal better than other doses. In addition, those doses can inhibit effectively H9N2 viral binding to red blood cells. This study suggested that the NanB sialidase of Pasteurella multocida B018 has a potent antiviral activity because can hydrolyze sialic acid on red blood cells surface and inhibit the H9N2 viral binding to the cells.
UR - http://www.scopus.com/inward/record.url?scp=85131638877&partnerID=8YFLogxK
U2 - 10.1038/s41598-022-13635-x
DO - 10.1038/s41598-022-13635-x
M3 - Article
C2 - 35676312
AN - SCOPUS:85131638877
VL - 12
JO - Scientific Reports
JF - Scientific Reports
SN - 2045-2322
IS - 1
M1 - 9425
ER -