T-even-type bacteriophages use an adhesin for recognition of cellular receptors |
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| Authors: | I Riede K Drexler H Schwarz U Henning |
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| Institution: | 1. Department of Radiation Oncology, School of Medicine, Washington University in St. Louis, St. Louis, Missouri, USA;1. Venenum Biodesign, a member of Genesis Biotechnology Group, 8 Black Forest Road, Hamilton, NJ 08691, USA;2. Femeris Women’s Health Research Center, a member of Genesis Biotechnology Group, 2000 Waterview Drive, Hamilton, NJ 08691, USA;1. New Mexico Veterans Administration Health Care System, 1501 San Pedro SE, Albuquerque, NM 87108, USA;2. School of Medicine, University of New Mexico, MSC10 5550, Albuquerque, NM 87131, USA;1. Molecular Structure & Function, The Hospital for Sick Children, 686 Bay Street, Toronto, ON M5G 0A4, Canada;2. Merck & Co. Inc., 2000 Galloping Hill Road, K15, Kenilworth, NJ 07033, USA;3. Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada |
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| Abstract: | Protein 38 of the Escherichia coli phage T4 is thought to be required catalytically for the assembly of the long tail fibers of this phage. It is shown that this protein of phage T2 and the T-even-type phage K3 and Ox2 act differently. It was found that NH2-terminal fragments of the protein, expressed from cloned fragments of gene 38 of phage K3, bind to gene 38 amber mutants of phage T2. Such phage or T2 gene 38 amber mutants, grown on a non-permissive host, possess a complete set of six tail fibers but are non-infectious. Both types of non-infectious phage could be repaired by incubation with an extract of cells harboring a cloned gene 38 of a host range mutant of phage K3, K3hx. The repaired phages had the host range of K3hx and not of T2. Immuno-electron microscopy showed that protein 38 is located at the free ends of the long tail fibers of phages T2, K3 and Ox2. The protein serves the recognition of the cellular receptor, i.e. it acts as an adhesin. |
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