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Heat-Denatured Lysozyme Inactivates Murine Norovirus as a Surrogate Human Norovirus.

Takahashi H, Nakazawa M, Ohshima C, Sato M, Tsuchiya T, Takeuchi A, Kunou M, Kuda T, Kimura B - Sci Rep (2015)

Bottom Line: Being highly infectious and highly viable in the environment, inactivation of the norovirus requires a highly effective inactivating agent.We observed that lysozymes heat-treated for 40 min at 100 °C caused a 4.5 log reduction in infectivity of norovirus.The amino acid sequence of the lysozyme was divided into three sections and the peptides of each artificially synthesised, in order to determine the region responsible for the inactivating effect.

View Article: PubMed Central - PubMed

Affiliation: Department of Food Science and Technology, Faculty of Marine Science, Tokyo University of Marine Science and Technology, 4 -5-7, Konan, Minato-ku, Tokyo, 108-8477 Japan.

ABSTRACT
Human norovirus infects humans through the consumption of contaminated food, contact with the excrement or vomit of an infected person, and through airborne droplets that scatter the virus through the air. Being highly infectious and highly viable in the environment, inactivation of the norovirus requires a highly effective inactivating agent. In this study, we have discovered the thermal denaturing capacity of a lysozyme with known antimicrobial activity against gram-positive bacteria, as well as its inactivating effect on murine norovirus. This study is the first report on the norovirus-inactivating effects of a thermally denatured lysozyme. We observed that lysozymes heat-treated for 40 min at 100 °C caused a 4.5 log reduction in infectivity of norovirus. Transmission electron microscope analysis showed that virus particles exposed to thermally denatured lysozymes were expanded, compared to the virus before exposure. The amino acid sequence of the lysozyme was divided into three sections and the peptides of each artificially synthesised, in order to determine the region responsible for the inactivating effect. These results suggest that thermal denaturation of the lysozyme changes the protein structure, activating the region responsible for imparting an inactivating effect against the virus.

No MeSH data available.


Related in: MedlinePlus

Antiviral activity of the partial amino acid sequence of Lysozyme obtained by artificial synthes.Significant difference was observed between Lz23-57 and Lz58-81(p < 0.01).
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f7: Antiviral activity of the partial amino acid sequence of Lysozyme obtained by artificial synthes.Significant difference was observed between Lz23-57 and Lz58-81(p < 0.01).

Mentions: Therefore, in order to investigate the amino acid sequence of lysozyme responsible for viral inactivation, we broadly divided the amino acid sequence of the lysozyme into three sections by the motif of secondary structure of lysozyme, and studied their respective MNV-inactivating abilities (Fig. 7). Of the peptides obtained by artificial synthesis, the first set displayed a higher inactivating effect, compared to that observed in the remaining two regions (58–81 residues, 98–132 residues). This peptide region reduced the infectivity of MNV by 2.6 log. The inactivating effect of the remaining two regions was 0.2 log and 0.3 log.


Heat-Denatured Lysozyme Inactivates Murine Norovirus as a Surrogate Human Norovirus.

Takahashi H, Nakazawa M, Ohshima C, Sato M, Tsuchiya T, Takeuchi A, Kunou M, Kuda T, Kimura B - Sci Rep (2015)

Antiviral activity of the partial amino acid sequence of Lysozyme obtained by artificial synthes.Significant difference was observed between Lz23-57 and Lz58-81(p < 0.01).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4488868&req=5

f7: Antiviral activity of the partial amino acid sequence of Lysozyme obtained by artificial synthes.Significant difference was observed between Lz23-57 and Lz58-81(p < 0.01).
Mentions: Therefore, in order to investigate the amino acid sequence of lysozyme responsible for viral inactivation, we broadly divided the amino acid sequence of the lysozyme into three sections by the motif of secondary structure of lysozyme, and studied their respective MNV-inactivating abilities (Fig. 7). Of the peptides obtained by artificial synthesis, the first set displayed a higher inactivating effect, compared to that observed in the remaining two regions (58–81 residues, 98–132 residues). This peptide region reduced the infectivity of MNV by 2.6 log. The inactivating effect of the remaining two regions was 0.2 log and 0.3 log.

Bottom Line: Being highly infectious and highly viable in the environment, inactivation of the norovirus requires a highly effective inactivating agent.We observed that lysozymes heat-treated for 40 min at 100 °C caused a 4.5 log reduction in infectivity of norovirus.The amino acid sequence of the lysozyme was divided into three sections and the peptides of each artificially synthesised, in order to determine the region responsible for the inactivating effect.

View Article: PubMed Central - PubMed

Affiliation: Department of Food Science and Technology, Faculty of Marine Science, Tokyo University of Marine Science and Technology, 4 -5-7, Konan, Minato-ku, Tokyo, 108-8477 Japan.

ABSTRACT
Human norovirus infects humans through the consumption of contaminated food, contact with the excrement or vomit of an infected person, and through airborne droplets that scatter the virus through the air. Being highly infectious and highly viable in the environment, inactivation of the norovirus requires a highly effective inactivating agent. In this study, we have discovered the thermal denaturing capacity of a lysozyme with known antimicrobial activity against gram-positive bacteria, as well as its inactivating effect on murine norovirus. This study is the first report on the norovirus-inactivating effects of a thermally denatured lysozyme. We observed that lysozymes heat-treated for 40 min at 100 °C caused a 4.5 log reduction in infectivity of norovirus. Transmission electron microscope analysis showed that virus particles exposed to thermally denatured lysozymes were expanded, compared to the virus before exposure. The amino acid sequence of the lysozyme was divided into three sections and the peptides of each artificially synthesised, in order to determine the region responsible for the inactivating effect. These results suggest that thermal denaturation of the lysozyme changes the protein structure, activating the region responsible for imparting an inactivating effect against the virus.

No MeSH data available.


Related in: MedlinePlus