Molecular characterization of an autolysin-defective mutant of Streptococcus pneumoniae |
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| Authors: | J L García J M Sánchez-Puelles P García R López C Ronda E García |
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| Institution: | 1. School of Pharmaceutical Sciences, Key Laboratory of Biotechnology and Pharmaceutical Engineering, Wenzhou Medical University, Wenzhou, Zhejiang, 325027, People''s Republic of China;2. Department of Orthopaedic Surgery, The Second Affiliated Hospital and Yuying Children''s Hospital of Wenzhou Medical University，Wenzhou, 325027, People''s Republic of China;3. Department of Postgraduate Education, Wenzhou Medical University, Wenzhou, 325027, People''s Republic of China;4. North Sichuan Medical College, Nanchong, 637000, People''s Republic of China;2. Department on Biomedical Chemistry, Research Unit of BioActive MoleculesInstitut de Química Avançada de Catalunya, 08034 Barcelona, Spain;4. Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y DigestivasInstituto de Salud Carlos III, E-28029 Madrid, Spain;11. Department of Biochemistry and Physiology, School of PharmacyInstitut de Biomedicina de la Universitat de Barcelona, Universitat de Barcelona, E-08028 Barcelona, Spain;3. Metchnikoff Laboratory, Dipartimento di Scienze Pediatriche, Ginecologiche, Microbiologiche e Biomediche (SPGMB), University of Messina, 98125 Messina, Italy;4. Institut Pasteur, Unité de Biologie des Bactéries Pathogènes à Gram Positif, CNRS ERL3526, 75015 Paris, France;5. Department of Molecular Medicine, Unit of Biochemistry, University of Pavia, 27100 Pavia, Italy |
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| Abstract: | The mutant gene lyt-4 of the autolysin-defective mutant R6ly4-4 of Streptococcus pneumoniae, which synthesized a temperature-sensitive autolytic enzyme, has been cloned in Escherichia coli. The nucleotide defect of the lyt-4 mutation has been characterized as a CG to TA transition. This transition causes the appearance of a glutamic acid instead of a glycine in the amino acid sequence of the autolysin, altering the hydropathic profile of the protein. This alteration might explain the observed thermosensitivity of the mutated autolytic enzyme. The present work represents the first molecular characterization of a mutation in the structural gene of a bacterial autolysin. |
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