-
Something wrong with this record ?
Ability of phages to infect Acinetobacter calcoaceticus-Acinetobacter baumannii complex species through acquisition of different pectate lyase depolymerase domains
H. Oliveira, AR. Costa, N. Konstantinides, A. Ferreira, E. Akturk, S. Sillankorva, A. Nemec, M. Shneider, A. Dötsch, J. Azeredo,
Language English Country England, Great Britain
Document type Journal Article
- MeSH
- Acinetobacter baumannii virology MeSH
- Acinetobacter calcoaceticus virology MeSH
- Genome, Viral genetics MeSH
- Host Specificity physiology MeSH
- Podoviridae classification genetics metabolism MeSH
- Polygalacturonase metabolism MeSH
- Polysaccharide-Lyases metabolism MeSH
- Protein Domains physiology MeSH
- Base Sequence MeSH
- Virion genetics MeSH
- Publication type
- Journal Article MeSH
- Geographicals
- Asia MeSH
- Europe MeSH
Bacteriophages are ubiquitous in nature and represent a vast repository of genetic diversity, which is driven by the endless coevolution cycle with a diversified group of bacterial hosts. Studying phage-host interactions is important to gain novel insights into their dynamic adaptation. In this study, we isolated 12 phages infecting species of the Acinetobacter baumannii-Acinetobacter calcoaceticus complex which exhibited a narrow host range and similar morphological features (podoviruses with short tails of 9-12 nm and isometric heads of 50-60 nm). Notably, the alignment of the newly sequenced phage genomes (40-41 kb of DNA length) and all Acinetobacter podoviruses deposited in Genbank has shown high synteny, regardless of the date and source of isolation that spans from America to Europe and Asia. Interestingly, the C-terminal pectate lyase domain of these phage tail fibres is often the only difference found among these viral genomes, demonstrating a very specific genomic variation during the course of their evolution. We proved that the pectate lyase domain is responsible for phage depolymerase activity and binding to specific Acinetobacter bacterial capsules. We discuss how this mechanism of phage-host co-evolution impacts the tail specificity apparatus of Acinetobacter podoviruses.
References provided by Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc18024527
- 003
- CZ-PrNML
- 005
- 20180712114913.0
- 007
- ta
- 008
- 180709s2017 enk f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1111/1462-2920.13970 $2 doi
- 035 __
- $a (PubMed)29076652
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a enk
- 100 1_
- $a Oliveira, Hugo $u CEB - Centre of Biological Engineering, LIBRO - Laboratório de Investigação em Biofilmes Rosário Oliveira, University of Minho, 4710-057 Braga, Portugal.
- 245 10
- $a Ability of phages to infect Acinetobacter calcoaceticus-Acinetobacter baumannii complex species through acquisition of different pectate lyase depolymerase domains / $c H. Oliveira, AR. Costa, N. Konstantinides, A. Ferreira, E. Akturk, S. Sillankorva, A. Nemec, M. Shneider, A. Dötsch, J. Azeredo,
- 520 9_
- $a Bacteriophages are ubiquitous in nature and represent a vast repository of genetic diversity, which is driven by the endless coevolution cycle with a diversified group of bacterial hosts. Studying phage-host interactions is important to gain novel insights into their dynamic adaptation. In this study, we isolated 12 phages infecting species of the Acinetobacter baumannii-Acinetobacter calcoaceticus complex which exhibited a narrow host range and similar morphological features (podoviruses with short tails of 9-12 nm and isometric heads of 50-60 nm). Notably, the alignment of the newly sequenced phage genomes (40-41 kb of DNA length) and all Acinetobacter podoviruses deposited in Genbank has shown high synteny, regardless of the date and source of isolation that spans from America to Europe and Asia. Interestingly, the C-terminal pectate lyase domain of these phage tail fibres is often the only difference found among these viral genomes, demonstrating a very specific genomic variation during the course of their evolution. We proved that the pectate lyase domain is responsible for phage depolymerase activity and binding to specific Acinetobacter bacterial capsules. We discuss how this mechanism of phage-host co-evolution impacts the tail specificity apparatus of Acinetobacter podoviruses.
- 650 _2
- $a Acinetobacter baumannii $x virologie $7 D040981
- 650 _2
- $a Acinetobacter calcoaceticus $x virologie $7 D016954
- 650 _2
- $a Asie $7 D001208
- 650 _2
- $a sekvence nukleotidů $7 D001483
- 650 _2
- $a Evropa $7 D005060
- 650 _2
- $a genom virový $x genetika $7 D016679
- 650 _2
- $a hostitelská specificita $x fyziologie $7 D058507
- 650 _2
- $a Podoviridae $x klasifikace $x genetika $x metabolismus $7 D017902
- 650 _2
- $a polygalakturonasa $x metabolismus $7 D011096
- 650 _2
- $a polysacharid-lyasy $x metabolismus $7 D011133
- 650 _2
- $a proteinové domény $x fyziologie $7 D000072417
- 650 _2
- $a virion $x genetika $7 D014771
- 655 _2
- $a časopisecké články $7 D016428
- 700 1_
- $a Costa, Ana R $u CEB - Centre of Biological Engineering, LIBRO - Laboratório de Investigação em Biofilmes Rosário Oliveira, University of Minho, 4710-057 Braga, Portugal.
- 700 1_
- $a Konstantinides, Nico $u CEB - Centre of Biological Engineering, LIBRO - Laboratório de Investigação em Biofilmes Rosário Oliveira, University of Minho, 4710-057 Braga, Portugal. Laboratory of Microbiology, Wageningen University, Stippeneng, 6708 WE Wageningen, The Netherlands.
- 700 1_
- $a Ferreira, Alice $u CEB - Centre of Biological Engineering, LIBRO - Laboratório de Investigação em Biofilmes Rosário Oliveira, University of Minho, 4710-057 Braga, Portugal.
- 700 1_
- $a Akturk, Ergun $u CEB - Centre of Biological Engineering, LIBRO - Laboratório de Investigação em Biofilmes Rosário Oliveira, University of Minho, 4710-057 Braga, Portugal.
- 700 1_
- $a Sillankorva, Sanna $u CEB - Centre of Biological Engineering, LIBRO - Laboratório de Investigação em Biofilmes Rosário Oliveira, University of Minho, 4710-057 Braga, Portugal.
- 700 1_
- $a Nemec, Alexandr $u Laboratory of Bacterial Genetics, National Institute of Public Health, Šrobárova 48, 100 42 Prague, Czech Republic.
- 700 1_
- $a Shneider, Mikhail $u Laboratory of Molecular Bioengineering, 16/10 Miklukho-Maklaya St, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 117997 Moscow, Russia.
- 700 1_
- $a Dötsch, Andreas $u Institute of Functional Interfaces, Karlsruhe Institute of Technology (KIT), Eggenstein-Leopoldshafen, Germany. Max Rubner-Institute, Institute for Physiologie and Biochemistry of Nutrition, Haid-und-Neu-Str. 9, 76131 Karlsruhe, Germany.
- 700 1_
- $a Azeredo, Joana $u CEB - Centre of Biological Engineering, LIBRO - Laboratório de Investigação em Biofilmes Rosário Oliveira, University of Minho, 4710-057 Braga, Portugal.
- 773 0_
- $w MED00007220 $t Environmental microbiology $x 1462-2920 $g Roč. 19, č. 12 (2017), s. 5060-5077
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/29076652 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20180709 $b ABA008
- 991 __
- $a 20180712115206 $b ABA008
- 999 __
- $a ok $b bmc $g 1316658 $s 1021448
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2017 $b 19 $c 12 $d 5060-5077 $e 20171204 $i 1462-2920 $m Environmental microbiology $n Environ Microbiol $x MED00007220
- LZP __
- $a Pubmed-20180709