vibrio strains Search Results


93
ATCC 17802d 5
Gene sources, primer sets for V-antigen and OprF gene cloning, and characteristics of the recombinant V-antigens and OprF used in this study.
17802d 5, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
ATCC atcc 33125
Gene sources, primer sets for V-antigen and OprF gene cloning, and characteristics of the recombinant V-antigens and OprF used in this study.
Atcc 33125, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
ATCC atcc 29307
Gene sources, primer sets for V-antigen and OprF gene cloning, and characteristics of the recombinant V-antigens and OprF used in this study.
Atcc 29307, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
ATCC atcc baa 1120 atcc
Gene sources, primer sets for V-antigen and OprF gene cloning, and characteristics of the recombinant V-antigens and OprF used in this study.
Atcc Baa 1120 Atcc, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
ATCC vibrio cholerae serotype o1
Structural alignment of the model of subunit NqrF from P. bryantii (red) and the structure of subunit NqrF from V. <t>cholerae</t> (gray, PDB 8A1W). A Subunit NqrF with two cytoplasmic domains harboring the FAD and [2Fe–2S] cofactors, respectively. B Close-up view of the FAD-binding domain. The conserved amino acids Tyr212, Ser213 and Phe406 in Vc-NqrF and Tyr216, Ser217 and Phe421 in Pb-NqrF coordinate the non-covalently bound FAD. C Close-up view of the [2Fe–2S] coordination. Four cysteines (Cys70, Cys76, Cys79 and Cys111 in Vc-NqrF; Cys69, Cys75, Cys78 and Cys110 in Pb-NqrF) coordinate the [2Fe–2S] with their sulfur residues (yellow-colored sticks). Cysteine rotamers of Pb-NqrF were adjusted to match the rotamers observed in Vc-NqrF. FAD is indicated in yellow, iron atoms are shown as orange spheres, and sulfur atoms as yellow spheres. The coordinates of the Vc-NqrF structure were obtained from the protein data bank (PDB 8A1W) and the Pb-NqrF structure was modeled with Phyre2. The structures were aligned and drawn with UCFS ChimeraX version 1.5
Vibrio Cholerae Serotype O1, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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92
ATCC v cholerae mo45 atcc 51394d 5
Structural alignment of the model of subunit NqrF from P. bryantii (red) and the structure of subunit NqrF from V. <t>cholerae</t> (gray, PDB 8A1W). A Subunit NqrF with two cytoplasmic domains harboring the FAD and [2Fe–2S] cofactors, respectively. B Close-up view of the FAD-binding domain. The conserved amino acids Tyr212, Ser213 and Phe406 in Vc-NqrF and Tyr216, Ser217 and Phe421 in Pb-NqrF coordinate the non-covalently bound FAD. C Close-up view of the [2Fe–2S] coordination. Four cysteines (Cys70, Cys76, Cys79 and Cys111 in Vc-NqrF; Cys69, Cys75, Cys78 and Cys110 in Pb-NqrF) coordinate the [2Fe–2S] with their sulfur residues (yellow-colored sticks). Cysteine rotamers of Pb-NqrF were adjusted to match the rotamers observed in Vc-NqrF. FAD is indicated in yellow, iron atoms are shown as orange spheres, and sulfur atoms as yellow spheres. The coordinates of the Vc-NqrF structure were obtained from the protein data bank (PDB 8A1W) and the Pb-NqrF structure was modeled with Phyre2. The structures were aligned and drawn with UCFS ChimeraX version 1.5
V Cholerae Mo45 Atcc 51394d 5, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
ATCC vibrio cholerae n16961
Structural alignment of the model of subunit NqrF from P. bryantii (red) and the structure of subunit NqrF from V. <t>cholerae</t> (gray, PDB 8A1W). A Subunit NqrF with two cytoplasmic domains harboring the FAD and [2Fe–2S] cofactors, respectively. B Close-up view of the FAD-binding domain. The conserved amino acids Tyr212, Ser213 and Phe406 in Vc-NqrF and Tyr216, Ser217 and Phe421 in Pb-NqrF coordinate the non-covalently bound FAD. C Close-up view of the [2Fe–2S] coordination. Four cysteines (Cys70, Cys76, Cys79 and Cys111 in Vc-NqrF; Cys69, Cys75, Cys78 and Cys110 in Pb-NqrF) coordinate the [2Fe–2S] with their sulfur residues (yellow-colored sticks). Cysteine rotamers of Pb-NqrF were adjusted to match the rotamers observed in Vc-NqrF. FAD is indicated in yellow, iron atoms are shown as orange spheres, and sulfur atoms as yellow spheres. The coordinates of the Vc-NqrF structure were obtained from the protein data bank (PDB 8A1W) and the Pb-NqrF structure was modeled with Phyre2. The structures were aligned and drawn with UCFS ChimeraX version 1.5
Vibrio Cholerae N16961, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
ATCC atcc 33149
Structural alignment of the model of subunit NqrF from P. bryantii (red) and the structure of subunit NqrF from V. <t>cholerae</t> (gray, PDB 8A1W). A Subunit NqrF with two cytoplasmic domains harboring the FAD and [2Fe–2S] cofactors, respectively. B Close-up view of the FAD-binding domain. The conserved amino acids Tyr212, Ser213 and Phe406 in Vc-NqrF and Tyr216, Ser217 and Phe421 in Pb-NqrF coordinate the non-covalently bound FAD. C Close-up view of the [2Fe–2S] coordination. Four cysteines (Cys70, Cys76, Cys79 and Cys111 in Vc-NqrF; Cys69, Cys75, Cys78 and Cys110 in Pb-NqrF) coordinate the [2Fe–2S] with their sulfur residues (yellow-colored sticks). Cysteine rotamers of Pb-NqrF were adjusted to match the rotamers observed in Vc-NqrF. FAD is indicated in yellow, iron atoms are shown as orange spheres, and sulfur atoms as yellow spheres. The coordinates of the Vc-NqrF structure were obtained from the protein data bank (PDB 8A1W) and the Pb-NqrF structure was modeled with Phyre2. The structures were aligned and drawn with UCFS ChimeraX version 1.5
Atcc 33149, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
ATCC v cholerae o1 biotype e1 tor strain mak757
Electron micrograph of five newly isolated V. <t>cholerae</t> O139 phages. (a) MAD-5; (b) VE-2; (c) CAL-3; (d) S-2; (e) MS-3. Bars, 100 nm.
V Cholerae O1 Biotype E1 Tor Strain Mak757, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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92
ATCC vibrio parahaemolyticus str eb 101
Electron micrograph of five newly isolated V. <t>cholerae</t> O139 phages. (a) MAD-5; (b) VE-2; (c) CAL-3; (d) S-2; (e) MS-3. Bars, 100 nm.
Vibrio Parahaemolyticus Str Eb 101, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
ATCC jcm 31412 t
Electron micrograph of five newly isolated V. <t>cholerae</t> O139 phages. (a) MAD-5; (b) VE-2; (c) CAL-3; (d) S-2; (e) MS-3. Bars, 100 nm.
Jcm 31412 T, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
ATCC v parahaemolyticus eb101
Electron micrograph of five newly isolated V. <t>cholerae</t> O139 phages. (a) MAD-5; (b) VE-2; (c) CAL-3; (d) S-2; (e) MS-3. Bars, 100 nm.
V Parahaemolyticus Eb101, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Gene sources, primer sets for V-antigen and OprF gene cloning, and characteristics of the recombinant V-antigens and OprF used in this study.

Journal: PLoS ONE

Article Title: Epidemiological survey of serum titers from adults against various Gram-negative bacterial V-antigens

doi: 10.1371/journal.pone.0220924

Figure Lengend Snippet: Gene sources, primer sets for V-antigen and OprF gene cloning, and characteristics of the recombinant V-antigens and OprF used in this study.

Article Snippet: vcrV , Vibrio parahaemolyticus , ATCC 17802D-5 , Bam HI Pst I , 5’- CGGGATCC ATGACGGATATGACAACAAC-3’ 5’- CTGCAG TTAAATGGCTCGTAGGATTTCTTG-3’ , 1,866 , VcrV , 619 , 68.3 , -.

Techniques: Clone Assay, Recombinant, Expressing, Plasmid Preparation

Structural alignment of the model of subunit NqrF from P. bryantii (red) and the structure of subunit NqrF from V. cholerae (gray, PDB 8A1W). A Subunit NqrF with two cytoplasmic domains harboring the FAD and [2Fe–2S] cofactors, respectively. B Close-up view of the FAD-binding domain. The conserved amino acids Tyr212, Ser213 and Phe406 in Vc-NqrF and Tyr216, Ser217 and Phe421 in Pb-NqrF coordinate the non-covalently bound FAD. C Close-up view of the [2Fe–2S] coordination. Four cysteines (Cys70, Cys76, Cys79 and Cys111 in Vc-NqrF; Cys69, Cys75, Cys78 and Cys110 in Pb-NqrF) coordinate the [2Fe–2S] with their sulfur residues (yellow-colored sticks). Cysteine rotamers of Pb-NqrF were adjusted to match the rotamers observed in Vc-NqrF. FAD is indicated in yellow, iron atoms are shown as orange spheres, and sulfur atoms as yellow spheres. The coordinates of the Vc-NqrF structure were obtained from the protein data bank (PDB 8A1W) and the Pb-NqrF structure was modeled with Phyre2. The structures were aligned and drawn with UCFS ChimeraX version 1.5

Journal: Archives of Microbiology

Article Title: Functionality of the Na + -translocating NADH:quinone oxidoreductase and quinol:fumarate reductase from Prevotella bryantii inferred from homology modeling

doi: 10.1007/s00203-023-03769-5

Figure Lengend Snippet: Structural alignment of the model of subunit NqrF from P. bryantii (red) and the structure of subunit NqrF from V. cholerae (gray, PDB 8A1W). A Subunit NqrF with two cytoplasmic domains harboring the FAD and [2Fe–2S] cofactors, respectively. B Close-up view of the FAD-binding domain. The conserved amino acids Tyr212, Ser213 and Phe406 in Vc-NqrF and Tyr216, Ser217 and Phe421 in Pb-NqrF coordinate the non-covalently bound FAD. C Close-up view of the [2Fe–2S] coordination. Four cysteines (Cys70, Cys76, Cys79 and Cys111 in Vc-NqrF; Cys69, Cys75, Cys78 and Cys110 in Pb-NqrF) coordinate the [2Fe–2S] with their sulfur residues (yellow-colored sticks). Cysteine rotamers of Pb-NqrF were adjusted to match the rotamers observed in Vc-NqrF. FAD is indicated in yellow, iron atoms are shown as orange spheres, and sulfur atoms as yellow spheres. The coordinates of the Vc-NqrF structure were obtained from the protein data bank (PDB 8A1W) and the Pb-NqrF structure was modeled with Phyre2. The structures were aligned and drawn with UCFS ChimeraX version 1.5

Article Snippet: We also searched for NQR and RNF by aligning the amino acid sequences of the NQR subunits from Vibrio cholerae serotype O1 (strain ATCC 39541) and of RnfB from Escherichia coli K12 to the corresponding genomes using the basic local alignment search tool BLAST (Mount ).

Techniques: Binding Assay

Structural alignment of the models of NqrD (purple) and NqrE (cyan) subunits from P. bryantii with the structures of the corresponding NqrD and NqrE subunits from V. cholerae (gray). A Subunits NqrD and NqrE each provide two cysteine residues for coordination of a [2Fe–2S] located at the interface of the two subunits. B Close-up view of the [2Fe–2S] cluster. The thiol groups (yellow) of the four cysteines (Cys29, Cys112 in Vc-NqrD and Cys26, Cys120 in Vc-NqrE; Cys30, Cys113 in Pb-NqrD and Cys26, Cys120 in Pb-NqrE) coordinate the [2Fe–2S] cluster (orange and yellow spheres). The coordinates of the Vc-NqrD and NqrE structures were obtained from the protein data bank (PDB 8A1W), and the Pb-NqrD and NqrE structures were modeled with Phyre2. The structures were aligned and drawn with UCFS ChimeraX version 1.5

Journal: Archives of Microbiology

Article Title: Functionality of the Na + -translocating NADH:quinone oxidoreductase and quinol:fumarate reductase from Prevotella bryantii inferred from homology modeling

doi: 10.1007/s00203-023-03769-5

Figure Lengend Snippet: Structural alignment of the models of NqrD (purple) and NqrE (cyan) subunits from P. bryantii with the structures of the corresponding NqrD and NqrE subunits from V. cholerae (gray). A Subunits NqrD and NqrE each provide two cysteine residues for coordination of a [2Fe–2S] located at the interface of the two subunits. B Close-up view of the [2Fe–2S] cluster. The thiol groups (yellow) of the four cysteines (Cys29, Cys112 in Vc-NqrD and Cys26, Cys120 in Vc-NqrE; Cys30, Cys113 in Pb-NqrD and Cys26, Cys120 in Pb-NqrE) coordinate the [2Fe–2S] cluster (orange and yellow spheres). The coordinates of the Vc-NqrD and NqrE structures were obtained from the protein data bank (PDB 8A1W), and the Pb-NqrD and NqrE structures were modeled with Phyre2. The structures were aligned and drawn with UCFS ChimeraX version 1.5

Article Snippet: We also searched for NQR and RNF by aligning the amino acid sequences of the NQR subunits from Vibrio cholerae serotype O1 (strain ATCC 39541) and of RnfB from Escherichia coli K12 to the corresponding genomes using the basic local alignment search tool BLAST (Mount ).

Techniques:

Structural alignments of the models of the NqrB (orange) and NqrC (green) subunits from P. bryantii with the structures of the corresponding NqrB and NqrC subunits from V. cholerae (gray). A Close-up view of the FMN binding site in NqrC with Thr225 (Vc-NqrC) and Thr185 (Pb-NqrC). B Close-up view of the FMN binding site in NqrB with Thr236 (Vc-NqrB) and Thr221 (Pb-NqrB). C Close-up view of the riboflavin-binding site in NqrB with Gly198, Asn200, Thr162, Ala205, Asn203, Phe342 and Asp346 as interaction partners of riboflavin in Vc-NqrB, and Gly172, Asn174, Thr136, Ala179, Asn177, Phe313 and Asp317 in Pb-NqrB. The coordinates of the Vc-NqrB and NqrC structures were obtained from the protein data bank (PDB 8A1W), and the Pb-NqrB and NqrC structures were modeled with Phyre2. The structures were aligned and drawn with UCFS ChimeraX version 1.5

Journal: Archives of Microbiology

Article Title: Functionality of the Na + -translocating NADH:quinone oxidoreductase and quinol:fumarate reductase from Prevotella bryantii inferred from homology modeling

doi: 10.1007/s00203-023-03769-5

Figure Lengend Snippet: Structural alignments of the models of the NqrB (orange) and NqrC (green) subunits from P. bryantii with the structures of the corresponding NqrB and NqrC subunits from V. cholerae (gray). A Close-up view of the FMN binding site in NqrC with Thr225 (Vc-NqrC) and Thr185 (Pb-NqrC). B Close-up view of the FMN binding site in NqrB with Thr236 (Vc-NqrB) and Thr221 (Pb-NqrB). C Close-up view of the riboflavin-binding site in NqrB with Gly198, Asn200, Thr162, Ala205, Asn203, Phe342 and Asp346 as interaction partners of riboflavin in Vc-NqrB, and Gly172, Asn174, Thr136, Ala179, Asn177, Phe313 and Asp317 in Pb-NqrB. The coordinates of the Vc-NqrB and NqrC structures were obtained from the protein data bank (PDB 8A1W), and the Pb-NqrB and NqrC structures were modeled with Phyre2. The structures were aligned and drawn with UCFS ChimeraX version 1.5

Article Snippet: We also searched for NQR and RNF by aligning the amino acid sequences of the NQR subunits from Vibrio cholerae serotype O1 (strain ATCC 39541) and of RnfB from Escherichia coli K12 to the corresponding genomes using the basic local alignment search tool BLAST (Mount ).

Techniques: Binding Assay

Electron micrograph of five newly isolated V. cholerae O139 phages. (a) MAD-5; (b) VE-2; (c) CAL-3; (d) S-2; (e) MS-3. Bars, 100 nm.

Journal:

Article Title: Development and Evaluation of a Phage Typing Scheme for Vibrio cholerae O139

doi:

Figure Lengend Snippet: Electron micrograph of five newly isolated V. cholerae O139 phages. (a) MAD-5; (b) VE-2; (c) CAL-3; (d) S-2; (e) MS-3. Bars, 100 nm.

Article Snippet: V. cholerae O1 biotype E1 Tor strain MAK757 (ATCC 51352), 10 E1 Tor strains (strains ATCC 51610 to ATCC 51619) that had been phage typed, V. cholerae O1 Classical biotype strain 569B, and V. cholerae 154 were resistant to these five O139 phages and caused lysis of V. cholerae O139 strains.

Techniques: Isolation

SDS-PAGE patterns of structural proteins of five newly isolated V. cholerae O139 phages stained with Coomassie brilliant blue. Lanes 1 and 8, molecular size marker (in kilobases); lane 2, MAD-5; lane 3, VE-2; lane 4, CAL-3; lane 5, S-2; lane 6, MS-3; lane 7, D-10.

Journal:

Article Title: Development and Evaluation of a Phage Typing Scheme for Vibrio cholerae O139

doi:

Figure Lengend Snippet: SDS-PAGE patterns of structural proteins of five newly isolated V. cholerae O139 phages stained with Coomassie brilliant blue. Lanes 1 and 8, molecular size marker (in kilobases); lane 2, MAD-5; lane 3, VE-2; lane 4, CAL-3; lane 5, S-2; lane 6, MS-3; lane 7, D-10.

Article Snippet: V. cholerae O1 biotype E1 Tor strain MAK757 (ATCC 51352), 10 E1 Tor strains (strains ATCC 51610 to ATCC 51619) that had been phage typed, V. cholerae O1 Classical biotype strain 569B, and V. cholerae 154 were resistant to these five O139 phages and caused lysis of V. cholerae O139 strains.

Techniques: SDS Page, Isolation, Staining, Marker

(a) Determination of antigenic relatedness among the five newly isolated V. cholerae O139 phages by ELISA. Anti-MAD-5 phage antiserum was used as the antibody, and five V. cholerae O139 phages along with E1 Tor phage D-10 were used as antigens (□, MAD-5; ×, VE-2; ■, CAL-3; ●, S-2; ○, MS-3; •, D-10). (b) Determination of antigenic relatedness among the five newly isolated V. cholerae O139 phages by ELISA. Anti-VE-2 antisera was used as the antibody, and five V. cholerae O139 phages along with E1 Tor phage D-10 were used as antigens (□, VE-2; ×, MAD-5; ●, CAL-3; ■, S-2; ○, MS-3; •, D-10).

Journal:

Article Title: Development and Evaluation of a Phage Typing Scheme for Vibrio cholerae O139

doi:

Figure Lengend Snippet: (a) Determination of antigenic relatedness among the five newly isolated V. cholerae O139 phages by ELISA. Anti-MAD-5 phage antiserum was used as the antibody, and five V. cholerae O139 phages along with E1 Tor phage D-10 were used as antigens (□, MAD-5; ×, VE-2; ■, CAL-3; ●, S-2; ○, MS-3; •, D-10). (b) Determination of antigenic relatedness among the five newly isolated V. cholerae O139 phages by ELISA. Anti-VE-2 antisera was used as the antibody, and five V. cholerae O139 phages along with E1 Tor phage D-10 were used as antigens (□, VE-2; ×, MAD-5; ●, CAL-3; ■, S-2; ○, MS-3; •, D-10).

Article Snippet: V. cholerae O1 biotype E1 Tor strain MAK757 (ATCC 51352), 10 E1 Tor strains (strains ATCC 51610 to ATCC 51619) that had been phage typed, V. cholerae O1 Classical biotype strain 569B, and V. cholerae 154 were resistant to these five O139 phages and caused lysis of V. cholerae O139 strains.

Techniques: Isolation, Enzyme-linked Immunosorbent Assay

Restriction endonuclease (HindIII) digestion patterns of DNA isolated from five newly isolated V. cholerae O139 phages. Lane 1, lambda phage DNA digested with HindIII; lane 2, MAD-5; lane 3, VE-2; lane 4, CAL-3; lane 5, S-2; lane 6, MS-3; lane 7, D-10. Numbers on the left are in kilobases.

Journal:

Article Title: Development and Evaluation of a Phage Typing Scheme for Vibrio cholerae O139

doi:

Figure Lengend Snippet: Restriction endonuclease (HindIII) digestion patterns of DNA isolated from five newly isolated V. cholerae O139 phages. Lane 1, lambda phage DNA digested with HindIII; lane 2, MAD-5; lane 3, VE-2; lane 4, CAL-3; lane 5, S-2; lane 6, MS-3; lane 7, D-10. Numbers on the left are in kilobases.

Article Snippet: V. cholerae O1 biotype E1 Tor strain MAK757 (ATCC 51352), 10 E1 Tor strains (strains ATCC 51610 to ATCC 51619) that had been phage typed, V. cholerae O1 Classical biotype strain 569B, and V. cholerae 154 were resistant to these five O139 phages and caused lysis of V. cholerae O139 strains.

Techniques: Isolation

Phage typing patterns observed with the five  V. cholerae  O139 phages

Journal:

Article Title: Development and Evaluation of a Phage Typing Scheme for Vibrio cholerae O139

doi:

Figure Lengend Snippet: Phage typing patterns observed with the five V. cholerae O139 phages

Article Snippet: V. cholerae O1 biotype E1 Tor strain MAK757 (ATCC 51352), 10 E1 Tor strains (strains ATCC 51610 to ATCC 51619) that had been phage typed, V. cholerae O1 Classical biotype strain 569B, and V. cholerae 154 were resistant to these five O139 phages and caused lysis of V. cholerae O139 strains.

Techniques:

Distribution of phage types of  V. cholerae  O139 in different cities in India

Journal:

Article Title: Development and Evaluation of a Phage Typing Scheme for Vibrio cholerae O139

doi:

Figure Lengend Snippet: Distribution of phage types of V. cholerae O139 in different cities in India

Article Snippet: V. cholerae O1 biotype E1 Tor strain MAK757 (ATCC 51352), 10 E1 Tor strains (strains ATCC 51610 to ATCC 51619) that had been phage typed, V. cholerae O1 Classical biotype strain 569B, and V. cholerae 154 were resistant to these five O139 phages and caused lysis of V. cholerae O139 strains.

Techniques: Isolation