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Two flagellotropic phages and one pilus-specific phage active against Asticcacaulis biprosthecum
J L Pate1, S J Petzold, T H Umbreit
1Department of Bacteriology, College of Agricultural and Life Sciences, University of Wisconsin, Madison, Wisconsin 53706, USA.
Abstract:
Three phages active against cells of Asticcacaulis biprosthecum attach to receptor sites located at the pole of the cell where pili, flagella, and holdfast are produced. Phage phiAcS2, a large phage with a prolate cylindrical head and flexible, noncontractile tail, attaches to flagella as well as to receptor sites at the pole of the cell. Attachment to flagella occurs at the region where head and tail of the phage are joined, leaving the distal end of the tail free for attachment to receptor sites at the cell surface. Phages phiAcM2 and phiAcM4, are identical in appearance to each other, possessing prolate cylindrical heads and flexible, noncontractile tails, and are smaller than phage phiAcS2. Phage phiAcM4, exhibits the same flagellotropic characteristic as described for phage phiAcS2, including the manner of attachment to flagella. Phage phiAcM2 has no affinity for flagella, but attaches by the distal end of the tail to pili and to receptor sites at the pole of the cell. Mechanical removal of flagella and pili protects against infection by all three phages. Studies with phage-resistant mutants and with KCN-treated cells suggest that pili are required for infection by both flagellotropic and pilus-specific phages.
Insights
Bacteriophages (viruses that infect bacteria) targeting Asticcacaulis biprosthecum utilize cell surface structures like flagella and pili for attachment. Pili are essential for infection by all studied phages, regardless of their specific attachment mechanism.
Area of Science:
- Microbiology
- Virology
- Bacteriology
Background:
- Asticcacaulis biprosthecum is a bacterium with distinct polar appendages including flagella and pili.
- Bacteriophages (phages) are viruses that infect bacteria and can be specific to certain bacterial hosts.
- Understanding phage-host interactions is crucial for microbial ecology and biotechnology.
Purpose of the Study:
- To investigate the attachment mechanisms of three bacteriophages (phiAcS2, phiAcM2, phiAcM4) targeting Asticcacaulis biprosthecum.
- To identify the specific cell surface receptors involved in phage infection.
- To determine the role of flagella and pili in phage entry.
Main Methods:
- Microscopic observation of phage-host cell attachment.
- Experiments involving mechanical removal of flagella and pili.
- Studies using phage-resistant mutants and KCN-treated cells.
Main Results:
- All three phages attach to receptor sites at the pole of Asticcacaacaulis biprosthecum cells.
- Phage phiAcS2 and phiAcM4 attach to flagella (flagellotropic) and also to polar receptor sites.
- Phage phiAcM2 attaches to pili and polar receptor sites, but not flagella.
- Removal of flagella and pili confers protection against all three phages.
- Pili are essential for infection by both flagellotropic and pilus-specific phages.
Conclusions:
- Phage attachment to Asticcacaulis biprosthecum is mediated by polar receptor sites, flagella, and pili.
- Pili play a critical role in the infection process for all studied phages.
- The specific attachment strategy varies among phages, with some exhibiting flagellotropic behavior.
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