The abstract is read at the publisher; the summary is JClub's.
Cryo-EM structures of mycobacteriophage D29 show a specialized capsid-portal junction with five gp19.1 bridges and a 13-subunit gp6 collar around a gp23–gp27 core.
- Why it matters: Structural organization and host-recognition mechanisms for broad-host-range mycobacteriophages remain unclear, limiting rational understanding of how these viruses assemble and engage mycobacteria.
- What they did: Using cryo-EM, the study resolved capsid, connector, tail tube, and baseplate, then tested host recognition with whole-cell binding and plaque-competition assays.
- The result: The gp6 collar forms a 6:13 symmetry mismatch via six distinct gp6–gp27 interfaces, and binding/competition results implicate the gp6 collar and flexible trimeric gp31 fiber in host recognition.
The findingWhy it mattersWhat they didThe result
AI summary of the abstract · may contain errors · not medical advice · read the paper.