Type

Journal Article

Authors

Douwe van Sinderen
Christian Cambillau
David Veesler
François P. Douillard
Stéphanie Blangy
Jennifer Mahony
Cecilia Bebeacua
Barry Collins

Subjects

Chemistry

Topics
recognition functional analysis cell device image resolution phage adsorption receptor

Structure and functional analysis of the host recognition device of lactococcal phage tuc2009. (2013)

Abstract Many phages employ a large heteropolymeric organelle located at the tip of the tail, termed the baseplate, for host recognition. Contrast electron microscopy (EM) of the lactococcal phage Tuc2009 baseplate and its host-binding subunits, the so-called tripods, allowed us to obtain a low-resolution structural image of this organelle. Structural comparisons between the baseplate of the related phage TP901-1 and that of Tuc2009 demonstrated that they are highly similar, except for the presence of an additional protein in the Tuc2009 baseplate (BppATuc2009), which is attached to the top of the Tuc2009 tripod structure. Recombinantly produced Tuc2009 or TP901-1 tripods were shown to bind specifically to their particular host cell surfaces and are capable of almost fully and specifically eliminating Tuc2009 or TP901-1 phage adsorption, respectively. In the case of Tuc2009, such adsorption-blocking ability was reduced in tripods that lacked BppATuc2009, indicating that this protein increases the binding specificity and/or affinity of the Tuc2009 tripod to its host receptor.
Collections Ireland -> University College Cork -> PubMed

Full list of authors on original publication

Douwe van Sinderen, Christian Cambillau, David Veesler, François P. Douillard, Stéphanie Blangy, Jennifer Mahony, Cecilia Bebeacua, Barry Collins

Experts in our system

1
Christian Cambillau
University College Cork
Total Publications: 18
 
2
Stéphanie Blangy
University College Cork
Total Publications: 4
 
3
Jennifer Mahony
University College Cork
Total Publications: 87
 
4
Barry Collins
University College Cork
Total Publications: 11