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E34 tail protein: its identification and purification and comparison with P22 tail
Author(s) -
Villafane Robert,
Zayas Milka
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a478
Subject(s) - bacteriophage , salmonella enterica , salmonella , phage display , computational biology , phagemid , biology , epitope , gene , genetics , chemistry , bacteria , antibody , escherichia coli
To understand in detail the interaction between lipopolysaccharide (LPS) and proteins, a molecular genetic approach using phage tail proteins has been employed. The tailspike proteins (TSPs) from Salmonella enterica serovar Typhimurium phage P22 and Salmonella enterica serovar Newington phage e34 which use the host LPS as their initial receptors, are being compared. These phages can not infect the others host cell (because of slight LPS differences). However, much has already been learned about the P22 TSP and our efforts are directed at understanding these interactions with the phage e34. Previous studies had already indicated that there was similarity between the well‐studied tail protein of Salmonella phage P22 and the e34TSP with respect to their phage associated properties. This study shows that the two TSPs share monoclonal epitopes in their N‐terminal regions. We also report the DNA sequence of the gene for the e34 TSP as well as reporting its purification, and initial characterization. In addition, some aspects of the structure of the e34 tailspike protein have been deduced. These studies were supported by the NIH through grants: NIH MBRS SO6 GM008239 and NIH RCMI G12 RR03050.