Reduced virulence of a Listeria monocytogenes phospholipase-deficient mutant obtained by transposon insertion into the zinc metalloprotease gene
| Autor: | J E Alouf, C Geoffroy, Patrick Berche, Jean-Louis Gaillard, Jean-Luc Beretti, J. Raveneau |
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| Rok vydání: | 1992 |
| Předmět: |
Transposable element
Immunology Mutant Blotting Western Virulence Phospholipase Biology medicine.disease_cause Microbiology Mice Listeria monocytogenes Western blot medicine Animals Insertion Metalloproteinase Mice Inbred ICR medicine.diagnostic_test Metalloendopeptidases Molecular biology Zinc Infectious Diseases Phospholipases Mutation DNA Transposable Elements Parasitology Female Rabbits Research Article |
| Zdroj: | Infection and immunity. 60(3) |
| ISSN: | 0019-9567 |
| Popis: | A phospholipase-deficient mutant, termed JL762, was obtained from a virulent strain of Listeria monocytogenes by screening a bank of 5,000 Tn1545 transposon-induced mutants on 2.5% egg yolk brain heart infusion agar. As previously shown (J. Mengaud, C. Geoffroy, and P. Cossart, Infect. Immun. 59:1043-1049, 1991), the transposon insertion took place inside the gene mpl, which encodes a zinc metalloprotease. By Western blot (immunoblot) analysis, we showed that loss of phospholipase activity was associated with loss of a 29-kDa zinc-dependent phosphatidylcholine-phospholipase C (PC-PLC) in culture supernatant of JL762 and of EGD-SmR incubated with ion chelator. As the parental strain, JL762 still produced in supernatants approximately 33-kDa proteins antigenically closely related to the 29-kDa PC-PLC. These results strongly suggest that the zinc metalloprotease of L. monocytogenes might play a role in the maturation of the 29-kDa PC-PLC. Although the uptake and the intracellular growth of bacteria were not affected in vitro, we found that the virulence of mutant JL762 was strongly impaired in the mouse. |
| Databáze: | OpenAIRE |
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