Sims, A. et al. Superinfection exclusion creates spatially distinct influenza virus populations. PLoS Biol. 21, e3001941 (2023).
Puck, T. T. & Lee, H. H. Mechanism of cell wall penetration by viruses: II. Demonstration of cyclic permeability change accompanying virus an infection of Escherichia coli B cells. J. Exp. Med. 101, 151–175 (1955).
McAllister, W. T. & Barrett, C. L. Superinfection exclusion by bacteriophage T7. J. Virol. 24, 709–711 (1977).
Zhang, X.-F. et al. A self-perpetuating repressive state of a viral replication protein blocks superinfection by the identical virus. PLoS Pathog. 13, e1006253 (2017).
Laliberte, J. P. & Moss, B. A novel mode of poxvirus superinfection exclusion that stops fusion of the lipid bilayers of viral and mobile membranes. J. Virol. 88, 9751–9768 (2014).
Doceul, V., Hollinshead, M., van der Linden, L. & Smith, G. L. Repulsion of superinfecting virions: a mechanism for speedy virus unfold. Science 327, 873–876 (2010).
Pedruzzi, I., Rosenbusch, J. P. & Locher, Ok. P. Inactivation in vitro of the Escherichia coli outer membrane protein FhuA by a phage T5-encoded lipoprotein. FEMS Microbiol. Lett. 168, 119–125 (1998).
Lu, M. J. & Henning, U. Superinfection exclusion by T-even-type coliphages. Developments Microbiol. 2, 137–139 (1994).
Cumby, N., Edwards, A. M., Davidson, A. R. & Maxwell, Ok. L. The bacteriophage HK97 gp15 moron ingredient encodes a novel superinfection exclusion protein. J. Bacteriol. 194, 5012–5019 (2012).
Cumby, N., Reimer, Ok., Mengin-Lecreulx, D., Davidson, A. R. & Maxwell, Ok. L. The phage tail tape measure protein, an internal membrane protein and a periplasmic chaperone play related roles within the genome injection technique of E. coli phage HK97. Mol. Microbiol. 96, 437–447 (2015).
Kuzio, J. & Kropinski, A. M. O-antigen conversion in Pseudomonas aeruginosa PAO1 by bacteriophage D3. J. Bacteriol. 155, 203–212 (1983).
Newton, G. J. et al. Three-component-mediated serotype conversion in Pseudomonas aeruginosa by bacteriophage D3. Mol. Microbiol. 39, 1237–1247 (2001).
Chung, I.-Y., Jang, H.-J., Bae, H.-W. & Cho, Y.-H. A phage protein that inhibits the bacterial ATPase required for sort IV pilus meeting. Proc. Natl Acad. Sci. USA 111, 11503–11508 (2014).
Shah, M. et al. A phage-encoded anti-activator inhibits quorum sensing in Pseudomonas aeruginosa. Mol. Cell 81, 571–583 (2021).
Burrows, L. L. Pseudomonas aeruginosa twitching motility: sort IV pili in motion. Annu. Rev. Microbiol. 66, 493–520 (2012).
O’Toole, G. A. & Kolter, R. Flagellar and twitching motility are vital for Pseudomonas aeruginosa biofilm improvement. Mol. Microbiol. 30, 295–304 (1998).
Bondy-Denomy, J. et al. Prophages mediate protection in opposition to phage an infection by means of numerous mechanisms. ISME J. 10, 2854–2866 (2016).
Tsao, Y.-F. et al. Phage morons play an essential function in Pseudomonas aeruginosa phenotypes. J. Bacteriol. 200, e00189-18 (2018).
Battesti, A. & Bouveret, E. The bacterial two-hybrid system primarily based on adenylate cyclase reconstitution in Escherichia coli. Strategies 58, 325–334 (2012).
Alm, R. A., Bodero, A. J., Free, P. D. & Mattick, J. S. Identification of a novel gene, pilZ, important for sort 4 fimbrial biogenesis in Pseudomonas aeruginosa. J. Bacteriol. 178, 46–53 (1996).
Kus, J. V., Tullis, E., Cvitkovitch, D. G. & Burrows, L. L. Vital variations in sort IV pilin allele distribution amongst Pseudomonas aeruginosa isolates from cystic fibrosis (CF) versus non-CF sufferers. Microbiology 150, 1315–1326 (2004).
Llontop, E. E. et al. The PilB-PilZ-FimX regulatory complicated of the kind IV pilus from Xanthomonas citri. PLoS Pathog. 17, e1009808 (2021).
Koch, M. D., Black, M. E., Han, E., Shaevitz, J. W. & Gitai, Z. Pseudomonas aeruginosa distinguishes surfaces by stiffness utilizing retraction of sort IV pili. Proc. Natl Acad. Sci. USA 119, e2119434119 (2022).
Chang, Y.-W. et al. Structure of the kind IVa pilus machine. Science 351, aad2001 (2016).
Koch, M. D., Fei, C., Wingreen, N. S., Shaevitz, J. W. & Gitai, Z. Aggressive binding of impartial extension and retraction motors explains the quantitative dynamics of sort IV pili. Proc. Natl Acad. Sci. USA 118, e2014926118 (2021).
González-Valdez, A., Servín-González, L., Juárez, Ok., Hernandez-Aligio, A. & Soberón-Chávez, G. The impact of particular rhlA-las-box mutations on DNA binding and gene activation by Pseudomonas aeruginosa quorum-sensing transcriptional regulators RhlR and LasR. FEMS Microbiol. Lett. 356, 217–225 (2014).
Whiteley, M. & Greenberg, E. P. Promoter specificity components in Pseudomonas aeruginosa quorum-sensing-controlled genes. J. Bacteriol. 183, 5529–5534 (2001).
Siehnel, R. et al. A novel regulator controls the activation threshold of quorum-regulated genes in Pseudomonas aeruginosa. Proc. Natl Acad. Sci. USA 107, 7916–7921 (2010).
Sztanko, Ok. M. et al. Prophages categorical a kind IV pilus part to supply anti-phage defence. Preprint at bioRxiv https://doi.org/10.1101/2024.03.29.587342 (2024).
Hao, Y., Murphy, Ok., Lo, R. Y., Khursigara, C. M. & Lam, J. S. Single-nucleotide polymorphisms discovered within the migA and wbpX glycosyltransferase genes account for the intrinsic lipopolysaccharide defects exhibited by Pseudomonas aeruginosa PA14. J. Bacteriol. 197, 2780–2791 (2015).
Robbins, P. W. & Uchida, T. Research on the chemical foundation of the phage conversion of O-antigens within the E-group Salmonellae. Biochemistry 1, 323–335 (1962).
Kupczok, A., Bailey, Z. M., Refardt, D. & Wendling, C. C. Co-transfer of functionally interdependent genes contributes to genome mosaicism in lambdoid phages. Microb. Genom. 8, mgen000915 (2022).
Egido, J. E., Costa, A. R., Aparicio-Maldonado, C., Haas, P.-J. & Brouns, S. J. J. Mechanisms and scientific significance of bacteriophage resistance. FEMS Microbiol. Rev. 46, fuab048 (2022).
Labrie, S. J., Samson, J. E. & Moineau, S. Bacteriophage resistance mechanisms. Nat. Rev. Microbiol. 8, 317–327 (2010).
Taylor, V. L., Fitzpatrick, A. D., Islam, Z. & Maxwell, Ok. L. The various impacts of phage morons on bacterial health and virulence. Adv. Virus Res. 103, 1–31 (2019).
Berryhill, B. A. et al. The e-book of Lambda doesn’t inform us that naturally occurring lysogens of Escherichia coli are more likely to be resistant in addition to immune. Proc. Natl Acad. Sci. USA 120, e2212121120 (2023).
Hancock, R. E., Hantke, Ok. & Braun, V. Iron transport of Escherichia coli Ok-12: involvement of the colicin B receptor and of a citrate-inducible protein. J. Bacteriol. 127, 1370–1375 (1976).
Samsonov, V. V., Samsonov, V. V. & Sineoky, S. P. DcrA and dcrB Escherichia coli genes can management DNA injection by phages particular for BtuB and FhuA receptors. Res. Microbiol. 153, 639–646 (2002).
Scandella, D. & Arber, W. Phage λ DNA injection into Escherichia coli pel− mutants is restored by mutations in phage genes V or H. Virology 69, 206–215 (1976).
De Smet, J. et al. Excessive protection metabolomics evaluation reveals phage-specific alterations to Pseudomonas aeruginosa physiology throughout an infection. ISME J. 10, 1823–1835 (2016).
Høyland-Kroghsbo, N. M. et al. Quorum sensing controls the Pseudomonas aeruginosa CRISPR-Cas adaptive immune system. Proc. Natl Acad. Sci. USA 114, 131–135 (2017).
Silpe, J. E. & Bassler, B. L. A bunch-produced quorum-sensing autoinducer controls a phage lysis-lysogeny choice. Cell 176, 268–280 (2019).
Hunter, M. & Fusco, D. Superinfection exclusion: a viral technique with short-term advantages and long-term drawbacks. PLoS Comput. Biol. 18, e1010125 (2022).
Weller, S. Ok. & Sawitzke, J. A. Recombination promoted by DNA viruses: phage λ to herpes simplex virus. Annu. Rev. Microbiol. 68, 237–258 (2014).
Learn, A. F. The evolution of virulence. Developments Microbiol. 2, 73–76 (1994).
Man, B. et al. HIV F/3′ orf encodes a phosphorylated GTP-binding protein resembling an oncogene product. Nature 330, 266–269 (1987).
Kwon, Y. et al. Structural foundation of CD4 downregulation by HIV-1 Nef. Nat. Struct. Mol. Biol. 27, 822–828 (2020).
Doron, S. et al. Systematic discovery of antiphage protection methods within the microbial pangenome. Science 359, eaar4120 (2018).
Georjon, H. & Bernheim, A. The extremely numerous antiphage defence methods of micro organism. Nat. Rev. Microbiol. 21, 686–700 (2023).
Hampton, H. G., Watson, B. N. J. & Fineran, P. C. The arms race between micro organism and their phage foes. Nature 577, 327–336 (2020).
Aziz, R. Ok. et al. The RAST server: speedy annotations utilizing subsystems know-how. BMC Genom. 9, 75 (2008).
Qiu, D., Damron, F. H., Mima, T., Schweizer, H. P. & Yu, H. D. PBAD-based shuttle vectors for practical evaluation of poisonous and extremely regulated genes in Pseudomonas and Burkholderia spp. and different micro organism. Appl. Environ. Microbiol. 74, 7422–7426 (2008).
Csörgő, B. et al. A compact Cascade-Cas3 system for focused genome engineering. Nat. Strategies 17, 1183–1190 (2020).
Hmelo, L. R. et al. Precision-engineering the Pseudomonas aeruginosa genome with two-step allelic change. Nat. Protoc. 10, 1820–1841 (2015).
Jiang, W., Bikard, D., Cox, D., Zhang, F. & Marraffini, L. A. RNA-guided modifying of bacterial genomes utilizing CRISPR-Cas methods. Nat. Biotechnol. 31, 233–239 (2013).
Farinha, M. A. & Kropinski, A. M. Building of broad-host-range plasmid vectors for straightforward seen choice and evaluation of promoters. J. Bacteriol. 172, 3496–3499 (1990).
Liberati, N. T. et al. An ordered, nonredundant library of Pseudomonas aeruginosa pressure PA14 transposon insertion mutants. Proc. Natl Acad. Sci. USA 103, 2833–2838 (2006).
Schneider, C. A., Rasband, W. S. & Eliceiri, Ok. W. NIH Picture to ImageJ: 25 years of picture evaluation. Nat. Strategies 9, 671–675 (2012).
McCallum, M. et al. PilN binding modulates the construction and binding companions of the Pseudomonas aeruginosa sort IVa pilus protein PilM. J. Biol. Chem. 291, 11003–11015 (2016).
Sayers, E. W. et al. Database sources of the nationwide middle for biotechnology data. Nucleic Acids Res. 50, D20–D26 (2022).
Xuan, G., Lin, H. & Wang, J. Expression of a phage-encoded Gp21 protein protects Pseudomonas aeruginosa in opposition to phage an infection. J. Virol. 96, e01769-21 (2022).
Kozyrev, D., Svarchevskiĭ, A., Zaĭtsev, E. & Rybchin, V. Lysogenic conversion induced by phages phi 80. I. An outline of the phenomenon and the cloning of the conversion gene. Genetika 18, 555–560 (1982).
Vostrov, A. A., Vostrukhina, O. A., Svarchevsky, A. N. & Rybchin, V. N. Proteins liable for lysogenic conversion attributable to coliphages N15 and phi80 are extremely homologous. J. Bacteriol. 178, 1484–1486 (1996).
Kulikov, E. E. et al. Equine intestinal O-Seroconverting temperate coliphage Hf4s: genomic and organic characterization. Appl. Environ. Microbiol. 87, e01124-21 (2021).
Perry, L. L. et al. Sequence evaluation of Escherichia coli O157:H7 bacteriophage ΦV10 and identification of a phage-encoded immunity protein that modifies the O157 antigen. FEMS Microbiol. Lett. 292, 182–186 (2009).
Wollin, R., Stocker, B. A. & Lindberg, A. A. Lysogenic conversion of Salmonella typhimurium bacteriophages A3 and A4 consists of O-acetylation of rhamnose of the repeating unit of the O-antigenic polysaccharide chain. J. Bacteriol. 169, 1003–1009 (1987).
Villafane, R., Zayas, M., Gilcrease, E. B., Kropinski, A. M. & Casjens, S. R. Genomic evaluation of bacteriophage ε34 of Salmonella enterica serovar Anatum (15+). BMC Microbiol. 8, 227 (2008).
Kim, M. & Ryu, S. Spontaneous and transient defence in opposition to bacteriophage by phase-variable glucosylation of O-antigen in Salmonella enterica serovar Typhimurium. Mol. Microbiol. 86, 411–425 (2012).
Kintz, E. et al. A BTP1 prophage gene current in invasive non-typhoidal Salmonella determines composition and size of the O-antigen of the lipopolysaccharide. Mol. Microbiol. 96, 263–275 (2015).
Woods, D. E., Jeddeloh, J. A. & Fritz, D. L. & DeShazer, D. Burkholderia thailandensisE125 harbors a temperate bacteriophage particular for Burkholderia mallei. J. Bacteriol. 184, 4003–4017 (2002).
Allison, G. E. & Verma, N. Ok. Serotype-converting bacteriophages and O-antigen modification in Shigella flexneri. Developments Microbiol. 8, 17–23 (2000).
Clark, C. A., Beltrame, J. & Manning, P. A. The oac gene encoding a lipopolysaccharide O-antigen acetylase maps adjoining to the integrase-encoding gene on the genome of Shigella flexneri bacteriophage Sf6. Gene 107, 43–52 (1991).
Steiger, H., Müller, U. & Bauer, G. Non-receptivity for ϰ phage of ϰ-lysogenic Serratia and reactions to superinfection of receptive cells with a mutant prophage. Mol. Gen. Genet. 114, 358–367 (1972).
Coetzee, J. N. Lysogenic conversion within the genus proteus. Nature 189, 946–947 (1961).
Bielmann, R. et al. Receptor binding proteins of Listeria monocytogenes bacteriophages A118 and P35 acknowledge serovar-specific teichoic acids. Virology 477, 110–118 (2015).
Williamson, S. J., McLaughlin, M. R. & Paul, J. H. Interplay of the ΦHSIC virus with its host: lysogeny or pseudolysogeny? Appl. Environ. Microbiol. 67, 1682–1688 (2001).
Bisen, P. S., Bagchi, S. N. & Audholia, S. Nitrate reductase exercise of a cyanobacterium Phormidium uncinatum after cyanophage LPP-1 an infection. FEMS Microbiol. Lett. 33, 69–72 (1986).
Ingmer, H., Gerlach, D. & Wolz, C. Temperate phages of Staphylococcus aureus. Microbiol. Spectr. https://doi.org/10.1128/microbiolspec.gpp3-0058-2018 (2019).
Solar, X., Göhler, A., Heller, Ok. J. & Neve, H. The ltp gene of temperate Streptococcus thermophilus phage TP-J34 confers superinfection exclusion to Streptococcus thermophilus and Lactococcus lactis. Virology 350, 146–157 (2006).