Esterified whey proteins can protect Lactococcus lactis against bacteriophage infection. Comparison with the effect of native basic proteins and L-polylysines.
Inhibitory action of basic esterified milk whey proteins [methylated (Met) or ethylated (Et) beta-lactoglobulin (BLG) and alpha-lactalbumin (ALA)], basic native proteins (chicken egg white lysozyme and calf thymus histone), and basic protein-like substances (L-polylysines) against the activity and replication of lactococcal bacteriophages (bIL66, bIL67, and bIL170) was tested. Chemical interactions of these proteins with phage DNA were determined as well as their protective effect on the growth of a laboratory plasmid-cured Lactococcus lactis subjected to an infection by the bacteriophages. All the proteins studied showed inhibitory activity against the three bacteriophages as tested by marked reduction of their lytic activities and decreasing the replication of studied phages. Histone and Met-BLG were more active toward bIL66 and bIL67, respectively, while both proteins were highly and equally active toward bIL170. Lysozyme showed lower antiviral activity. Antiviral activity of Et-BLG was a little bit lower than that observed in the case of the Met derivative. Esterified ALA also showed considerable but slightly lower antiviral activity as compared to other proteins. L-polylysines also showed an antiviral effect against the three bacteriophages studied, their influence being highly dependent on their molecular size. The best effective size of L-polylysines was in the range 15-70 kDa. Replication of bIL67 was inhibited by the presence of esterified ALA or BLG and native basic proteins. Complete inhibition of replication of bIL67 occurred when using polylysines with molecular masses in the ranges 4-15, 15-30, and 30-70 kDa, while protein-like substrates with lower molecular masses had only a slight effect. The presence of histone and Met-BLG at a concentration of 0.13 mg/mL in the incubation medium protected L. lactis against lysis when it was subjected to an infection by bIL67 (10(5) pfu/mL). The same action was achieved by l-polylysine (15-30 kDa) used at a concentration of 0.03 mg/mL in the incubation medium.
Sitohy
Mahmoud
M
Laboratoire d'Etude des Interactions des Molécules Alimentaires, Institut National de la Recherche Agronomique, B.P. 71627, 44316 Nantes Cedex 3, France.
Chobert
Jean-Marc
JM
Haertlé
Thomas
T
D001435:Bacteriophages / Q000502:physiology*; D004951:Esterification; D006657:Histones / Q000494:pharmacology; D007768:Lactalbumin / Q000737:chemistry / Q000494:pharmacology; D013294:Lactococcus lactis / Q000254:growth & development / Q000821:virology*; D007782:Lactoglobulins / Q000737:chemistry / Q000494:pharmacology; D008894:Milk Proteins / Q000737:chemistry* / Q000494:pharmacology; D009113:Muramidase / Q000494:pharmacology; D011107:Polylysine / Q000494:pharmacology*; D011506:Proteins / Q000494:pharmacology*; D014779:Virus Replication / Q000187:drug effects; D000067816:Whey Proteins
D006657:Histones; D007782:Lactoglobulins; D008894:Milk Proteins; D011506:Proteins; D000067816:Whey Proteins; D011107:Polylysine; D007768:Lactalbumin; D009113:Muramidase