A hybrid receptor binding protein enables phage F341 infection of Campylobacter by binding to flagella and lipooligosaccharides
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A hybrid receptor binding protein enables phage F341 infection of Campylobacter by binding to flagella and lipooligosaccharides. / Ostenfeld, Line Jensen; Sørensen, Anders Nørgaard; Neve, Horst; Vitt, Amira; Klumpp, Jochen; Sørensen, Martine Camilla Holst.
In: Frontiers in Microbiology, Vol. 15, 1358909, 2024.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - A hybrid receptor binding protein enables phage F341 infection of Campylobacter by binding to flagella and lipooligosaccharides
AU - Ostenfeld, Line Jensen
AU - Sørensen, Anders Nørgaard
AU - Neve, Horst
AU - Vitt, Amira
AU - Klumpp, Jochen
AU - Sørensen, Martine Camilla Holst
N1 - Publisher Copyright: Copyright © 2024 Ostenfeld, Sørensen, Neve, Vitt, Klumpp and Sørensen.
PY - 2024
Y1 - 2024
N2 - Flagellotropic bacteriophages are interesting candidates as therapeutics against pathogenic bacteria dependent on flagellar motility for colonization and causing disease. Yet, phage resistance other than loss of motility has been scarcely studied. Here we developed a soft agar assay to study flagellotropic phage F341 resistance in motile Campylobacter jejuni. We found that phage adsorption was prevented by diverse genetic mutations in the lipooligosaccharides forming the secondary receptor of phage F341. Genome sequencing showed phage F341 belongs to the Fletchervirus genus otherwise comprising capsular-dependent C. jejuni phages. Interestingly, phage F341 encodes a hybrid receptor binding protein (RBP) predicted as a short tail fiber showing partial similarity to RBP1 encoded by capsular-dependent Fletchervirus, but with a receptor binding domain similar to tail fiber protein H of C. jejuni CJIE1 prophages. Thus, C. jejuni prophages may represent a genetic pool from where lytic Fletchervirus phages can acquire new traits like recognition of new receptors.
AB - Flagellotropic bacteriophages are interesting candidates as therapeutics against pathogenic bacteria dependent on flagellar motility for colonization and causing disease. Yet, phage resistance other than loss of motility has been scarcely studied. Here we developed a soft agar assay to study flagellotropic phage F341 resistance in motile Campylobacter jejuni. We found that phage adsorption was prevented by diverse genetic mutations in the lipooligosaccharides forming the secondary receptor of phage F341. Genome sequencing showed phage F341 belongs to the Fletchervirus genus otherwise comprising capsular-dependent C. jejuni phages. Interestingly, phage F341 encodes a hybrid receptor binding protein (RBP) predicted as a short tail fiber showing partial similarity to RBP1 encoded by capsular-dependent Fletchervirus, but with a receptor binding domain similar to tail fiber protein H of C. jejuni CJIE1 prophages. Thus, C. jejuni prophages may represent a genetic pool from where lytic Fletchervirus phages can acquire new traits like recognition of new receptors.
KW - Campylobacter
KW - flagella
KW - flagellotropic phage
KW - Fletchervirus
KW - phage
KW - phage receptor
KW - phage resistance
KW - receptor binding protein
U2 - 10.3389/fmicb.2024.1358909
DO - 10.3389/fmicb.2024.1358909
M3 - Journal article
C2 - 38380094
AN - SCOPUS:85185472814
VL - 15
JO - Frontiers in Microbiology
JF - Frontiers in Microbiology
SN - 1664-302X
M1 - 1358909
ER -
ID: 391510311