An antibacterial and antiviral peptide produced by Enterococcus mundtii ST4V isolated from soya beans
Enterococcus mundtii ST4V, isolated from soya beans, produces a 3950 Da antibacterial peptide active against Gram-positive and Gram-negative bacteria, including Enterococcus faecalis, Streptococcus spp., Pseudomonas aeruginosa, Klebsiella pneumoniae, Streptococcus pneumoniae and Staphylococcus aureu...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_09248579_v25_n6_p508_Todorov |
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todo:paper_09248579_v25_n6_p508_Todorov2023-10-03T15:46:05Z An antibacterial and antiviral peptide produced by Enterococcus mundtii ST4V isolated from soya beans Todorov, S.D. Wachsman, M.B. Knoetze, H. Meincken, M. Dicks, L.M.T. Antibacterial and antiviral peptide Enterococcus mundtii amylase pepsin A peptide ST4V polypeptide antibiotic agent pronase proteinase K trypsin unclassified drug animal cell antibacterial activity antiviral activity article bacterium isolation controlled study cytotoxicity drug isolation drug mechanism drug purification Enterococcus enterococcus mundtii nonhuman priority journal soybean Vero cell virus inactivation Animals Anti-Bacterial Agents Antiviral Agents Bacterial Proteins Cercopithecus aethiops Enterococcus Gram-Negative Bacteria Gram-Positive Bacteria Microbial Sensitivity Tests Peptide Hydrolases Soybeans Vero Cells Virus Inactivation Viruses Enterococcus mundtii ST4V, isolated from soya beans, produces a 3950 Da antibacterial peptide active against Gram-positive and Gram-negative bacteria, including Enterococcus faecalis, Streptococcus spp., Pseudomonas aeruginosa, Klebsiella pneumoniae, Streptococcus pneumoniae and Staphylococcus aureus. The peptide also inactivated the herpes simplex viruses HSV-1 (strain F) and HSV-2 (strain G), a polio virus (PV3, strain Sabin) and a measles virus (strain MV/BRAZIL/001/91, an attenuated strain of MV). MV, HSV-1 and HSV-2 were 95.5%-99.9% inactivated by peptide ST4V at 400 μg/ml. Monkey kidney Vero cells were not inactivated, even at four times the level peptide ST4V displayed antiviral activity, indicating that the effect was not due to cytotoxicity. Complete inactivation or significant reduction in antimicrobial activity was observed after treatment of peptide ST4V with Proteinase K, pronase, pepsin and trypsin. No change in antimicrobial activity was recorded after treatment with α-amylase, suggesting that peptide ST4V was not glycosylated. This is the first description of an antibacterial and antiviral peptide with such broad-spectrum of activity, produced by a lactic acid bacterium. © 2005 Elsevier B.V. and the International Society of Chemotherapy. All rights reserved. Fil:Wachsman, M.B. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_09248579_v25_n6_p508_Todorov |
| institution |
Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Antibacterial and antiviral peptide Enterococcus mundtii amylase pepsin A peptide ST4V polypeptide antibiotic agent pronase proteinase K trypsin unclassified drug animal cell antibacterial activity antiviral activity article bacterium isolation controlled study cytotoxicity drug isolation drug mechanism drug purification Enterococcus enterococcus mundtii nonhuman priority journal soybean Vero cell virus inactivation Animals Anti-Bacterial Agents Antiviral Agents Bacterial Proteins Cercopithecus aethiops Enterococcus Gram-Negative Bacteria Gram-Positive Bacteria Microbial Sensitivity Tests Peptide Hydrolases Soybeans Vero Cells Virus Inactivation Viruses |
| spellingShingle |
Antibacterial and antiviral peptide Enterococcus mundtii amylase pepsin A peptide ST4V polypeptide antibiotic agent pronase proteinase K trypsin unclassified drug animal cell antibacterial activity antiviral activity article bacterium isolation controlled study cytotoxicity drug isolation drug mechanism drug purification Enterococcus enterococcus mundtii nonhuman priority journal soybean Vero cell virus inactivation Animals Anti-Bacterial Agents Antiviral Agents Bacterial Proteins Cercopithecus aethiops Enterococcus Gram-Negative Bacteria Gram-Positive Bacteria Microbial Sensitivity Tests Peptide Hydrolases Soybeans Vero Cells Virus Inactivation Viruses Todorov, S.D. Wachsman, M.B. Knoetze, H. Meincken, M. Dicks, L.M.T. An antibacterial and antiviral peptide produced by Enterococcus mundtii ST4V isolated from soya beans |
| topic_facet |
Antibacterial and antiviral peptide Enterococcus mundtii amylase pepsin A peptide ST4V polypeptide antibiotic agent pronase proteinase K trypsin unclassified drug animal cell antibacterial activity antiviral activity article bacterium isolation controlled study cytotoxicity drug isolation drug mechanism drug purification Enterococcus enterococcus mundtii nonhuman priority journal soybean Vero cell virus inactivation Animals Anti-Bacterial Agents Antiviral Agents Bacterial Proteins Cercopithecus aethiops Enterococcus Gram-Negative Bacteria Gram-Positive Bacteria Microbial Sensitivity Tests Peptide Hydrolases Soybeans Vero Cells Virus Inactivation Viruses |
| description |
Enterococcus mundtii ST4V, isolated from soya beans, produces a 3950 Da antibacterial peptide active against Gram-positive and Gram-negative bacteria, including Enterococcus faecalis, Streptococcus spp., Pseudomonas aeruginosa, Klebsiella pneumoniae, Streptococcus pneumoniae and Staphylococcus aureus. The peptide also inactivated the herpes simplex viruses HSV-1 (strain F) and HSV-2 (strain G), a polio virus (PV3, strain Sabin) and a measles virus (strain MV/BRAZIL/001/91, an attenuated strain of MV). MV, HSV-1 and HSV-2 were 95.5%-99.9% inactivated by peptide ST4V at 400 μg/ml. Monkey kidney Vero cells were not inactivated, even at four times the level peptide ST4V displayed antiviral activity, indicating that the effect was not due to cytotoxicity. Complete inactivation or significant reduction in antimicrobial activity was observed after treatment of peptide ST4V with Proteinase K, pronase, pepsin and trypsin. No change in antimicrobial activity was recorded after treatment with α-amylase, suggesting that peptide ST4V was not glycosylated. This is the first description of an antibacterial and antiviral peptide with such broad-spectrum of activity, produced by a lactic acid bacterium. © 2005 Elsevier B.V. and the International Society of Chemotherapy. All rights reserved. |
| format |
JOUR |
| author |
Todorov, S.D. Wachsman, M.B. Knoetze, H. Meincken, M. Dicks, L.M.T. |
| author_facet |
Todorov, S.D. Wachsman, M.B. Knoetze, H. Meincken, M. Dicks, L.M.T. |
| author_sort |
Todorov, S.D. |
| title |
An antibacterial and antiviral peptide produced by Enterococcus mundtii ST4V isolated from soya beans |
| title_short |
An antibacterial and antiviral peptide produced by Enterococcus mundtii ST4V isolated from soya beans |
| title_full |
An antibacterial and antiviral peptide produced by Enterococcus mundtii ST4V isolated from soya beans |
| title_fullStr |
An antibacterial and antiviral peptide produced by Enterococcus mundtii ST4V isolated from soya beans |
| title_full_unstemmed |
An antibacterial and antiviral peptide produced by Enterococcus mundtii ST4V isolated from soya beans |
| title_sort |
antibacterial and antiviral peptide produced by enterococcus mundtii st4v isolated from soya beans |
| url |
http://hdl.handle.net/20.500.12110/paper_09248579_v25_n6_p508_Todorov |
| work_keys_str_mv |
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