The Analysis of OmpA and Rz/Rz1 of Lytic Bacteriophage from Surabaya, Indonesia
A good strategy to conquer the Escherichia coli-cause food-borne disease could be bacteriophages. Porins are a type of β-barrel proteins with diffuse channels and OmpA, which has a role in hydrophilic transport, is the most frequent porin in E. coli; it was also chosen as the potential receptor of t...
Saved in:
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Wiley
2021-01-01
|
| Series: | Scientifica |
| Online Access: | http://dx.doi.org/10.1155/2021/7494144 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1850176319436881920 |
|---|---|
| author | Tessa Sjahriani Eddy Bagus Wasito Wiwiek Tyasningsih |
| author_facet | Tessa Sjahriani Eddy Bagus Wasito Wiwiek Tyasningsih |
| author_sort | Tessa Sjahriani |
| collection | DOAJ |
| description | A good strategy to conquer the Escherichia coli-cause food-borne disease could be bacteriophages. Porins are a type of β-barrel proteins with diffuse channels and OmpA, which has a role in hydrophilic transport, is the most frequent porin in E. coli; it was also chosen as the potential receptor of the phage. And the Rz/Rz1 was engaged in the breakup of the host bacterial external membrane. This study aimed to analyze the amino acid of OmpA and Rz/Rz1 of lytic bacteriophage from Surabaya, Indonesia. This study employed a sample of 8 bacteriophages from the previous study. The OmpA analysis method was mass spectrometry. Rz/Rz1 was analyzed using PCR, DNA sequencing, Expasy Translation, and Expasy ProtParam. The result obtained 10% to 29% sequence coverage of OmpA, carrying the ligand-binding site. The Rz/Rz1 gene shares a high percentage of 97.04% to 98.89% identities with the Siphoviridae isolate ctTwQ4, partial genome, and Myoviridae isolate cthRA4, partial genome. The Mann–Whitney statistical tests indicate the significant differences between Alanine, Aspartate, Glycine, Proline, Serine (p=0.011), Asparagine, Cysteine (p=0.009), Isoleucine (p=0.043), Lysine (p=0.034), Methionine (p=0.001), Threonine (p=0.018), and Tryptophan (p=0.007) of OmpA and Rz/Rz1. The conclusion obtained from this study is the fact that OmpA acts as Phage 1, Phage 2, Phage 3, Phage 5, and Phage 6 receptors for its peptide composition comprising the ligand binding site, and Rz/Rz1 participates in host bacteria lysis. |
| format | Article |
| id | doaj-art-b07f95e3aee342799801781a01d35162 |
| institution | OA Journals |
| issn | 2090-908X |
| language | English |
| publishDate | 2021-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Scientifica |
| spelling | doaj-art-b07f95e3aee342799801781a01d351622025-08-20T02:19:16ZengWileyScientifica2090-908X2021-01-01202110.1155/2021/7494144The Analysis of OmpA and Rz/Rz1 of Lytic Bacteriophage from Surabaya, IndonesiaTessa Sjahriani0Eddy Bagus Wasito1Wiwiek Tyasningsih2Doctoral ProgramDepartment of MicrobiologyDepartment of MicrobiologyA good strategy to conquer the Escherichia coli-cause food-borne disease could be bacteriophages. Porins are a type of β-barrel proteins with diffuse channels and OmpA, which has a role in hydrophilic transport, is the most frequent porin in E. coli; it was also chosen as the potential receptor of the phage. And the Rz/Rz1 was engaged in the breakup of the host bacterial external membrane. This study aimed to analyze the amino acid of OmpA and Rz/Rz1 of lytic bacteriophage from Surabaya, Indonesia. This study employed a sample of 8 bacteriophages from the previous study. The OmpA analysis method was mass spectrometry. Rz/Rz1 was analyzed using PCR, DNA sequencing, Expasy Translation, and Expasy ProtParam. The result obtained 10% to 29% sequence coverage of OmpA, carrying the ligand-binding site. The Rz/Rz1 gene shares a high percentage of 97.04% to 98.89% identities with the Siphoviridae isolate ctTwQ4, partial genome, and Myoviridae isolate cthRA4, partial genome. The Mann–Whitney statistical tests indicate the significant differences between Alanine, Aspartate, Glycine, Proline, Serine (p=0.011), Asparagine, Cysteine (p=0.009), Isoleucine (p=0.043), Lysine (p=0.034), Methionine (p=0.001), Threonine (p=0.018), and Tryptophan (p=0.007) of OmpA and Rz/Rz1. The conclusion obtained from this study is the fact that OmpA acts as Phage 1, Phage 2, Phage 3, Phage 5, and Phage 6 receptors for its peptide composition comprising the ligand binding site, and Rz/Rz1 participates in host bacteria lysis.http://dx.doi.org/10.1155/2021/7494144 |
| spellingShingle | Tessa Sjahriani Eddy Bagus Wasito Wiwiek Tyasningsih The Analysis of OmpA and Rz/Rz1 of Lytic Bacteriophage from Surabaya, Indonesia Scientifica |
| title | The Analysis of OmpA and Rz/Rz1 of Lytic Bacteriophage from Surabaya, Indonesia |
| title_full | The Analysis of OmpA and Rz/Rz1 of Lytic Bacteriophage from Surabaya, Indonesia |
| title_fullStr | The Analysis of OmpA and Rz/Rz1 of Lytic Bacteriophage from Surabaya, Indonesia |
| title_full_unstemmed | The Analysis of OmpA and Rz/Rz1 of Lytic Bacteriophage from Surabaya, Indonesia |
| title_short | The Analysis of OmpA and Rz/Rz1 of Lytic Bacteriophage from Surabaya, Indonesia |
| title_sort | analysis of ompa and rz rz1 of lytic bacteriophage from surabaya indonesia |
| url | http://dx.doi.org/10.1155/2021/7494144 |
| work_keys_str_mv | AT tessasjahriani theanalysisofompaandrzrz1oflyticbacteriophagefromsurabayaindonesia AT eddybaguswasito theanalysisofompaandrzrz1oflyticbacteriophagefromsurabayaindonesia AT wiwiektyasningsih theanalysisofompaandrzrz1oflyticbacteriophagefromsurabayaindonesia AT tessasjahriani analysisofompaandrzrz1oflyticbacteriophagefromsurabayaindonesia AT eddybaguswasito analysisofompaandrzrz1oflyticbacteriophagefromsurabayaindonesia AT wiwiektyasningsih analysisofompaandrzrz1oflyticbacteriophagefromsurabayaindonesia |