Resistance of
            <i>Klebsiella pneumoniae</i>
            to Phage hvKpP3 Due to High-Molecular Weight Lipopolysaccharide Synthesis Failure

Geng, Huaixin; Song, Lingjie; Yang, Xianggui; Xing, Siyu; Wang, Rui; Xü, Ying; Xu, Jin; Luan, Guangxin

doi:10.1128/spectrum.04384-22

Cited by 4 publications

(1 citation statement)

References 38 publications

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“…After the sequencing verification, recombinant plasmids were heat-shocked into expression receptor E. coli BL21 cells. Expressed glutathione S-transferase (GST)-tagged recombinant phage tail tubular proteins B induced by isopropylbeta-D-thiogalactopyranoside (IPTG) were purified on the glutathione-agarose columns and then analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in an 8% gel (Geng et al, 2023).…”

Section: Protein Expression and Molecular Modelingmentioning

confidence: 99%

Host range expansion of Acinetobacter phage vB_Ab4_Hep4 driven by a spontaneous tail tubular mutation

He,

Cao,

et al. 2024

Front. Cell. Infect. Microbiol.

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Bacteriophages (phages) represent promising alternative treatments against multidrug-resistant Acinetobacter baumannii (MDRAB) infections. The application of phages as antibacterial agents is limited by their generally narrow host ranges, so changing or expanding the host ranges of phages is beneficial for phage therapy. Multiple studies have identified that phage tail fiber protein mediates the recognition and binding to the host as receptor binding protein in phage infection. However, the tail tubular-dependent host specificity of phages has not been studied well. In this study, we isolated and characterized a novel lytic phage, vB_Ab4_Hep4, specifically infecting MDRAB strains. Meanwhile, we identified a spontaneous mutant of the phage, vB_Ab4_Hep4-M, which revealed an expanded host range compared to the wild-type phage. A single mutation of G to C was detected in the gene encoding the phage tail tubular protein B and thus resulted in an aspartate to histidine change. We further demonstrated that the host range expansion of the phage mutant is driven by the spontaneous mutation of guanine to cytosine using expressed tail tubular protein B. Moreover, we established that the bacterial capsule is the receptor for phage Abp4 and Abp4-M by identifying mutant genes in phage-resistant strains. In conclusion, our study provided a detailed description of phage vB_Ab4_Hep4 and revealed the tail tubular-dependent host specificity in A. baumannii phages, which may provide new insights into extending the host ranges of phages by gene-modifying tail tubular proteins.

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Section: Protein Expression and Molecular Modelingmentioning

confidence: 99%

Host range expansion of Acinetobacter phage vB_Ab4_Hep4 driven by a spontaneous tail tubular mutation

He,

Cao,

et al. 2024

Front. Cell. Infect. Microbiol.

Self Cite

View full text Add to dashboard Cite

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Bacteriophage-resistant carbapenem-resistant Klebsiella pneumoniae shows reduced antibiotic resistance and virulence

Chen,

Zhang,

Bai

et al. 2024

International Journal of Antimicrobial Agents

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Clinical and laboratory insights into the threat of hypervirulent Klebsiella pneumoniae

Han,

Yao,

et al. 2024

International Journal of Antimicrobial Agents

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Resistance of Klebsiella pneumoniae to Phage hvKpP3 Due to High-Molecular Weight Lipopolysaccharide Synthesis Failure

Abstract: Multidrug-resistant (MDR) Klebsiella pneumoniae strains pose a particular threat to human health. Therefore, it is very important for us to isolate phage and overcome phage resistance.

Cited by 4 publications

References 38 publications

Host range expansion of Acinetobacter phage vB_Ab4_Hep4 driven by a spontaneous tail tubular mutation

Host range expansion of Acinetobacter phage vB_Ab4_Hep4 driven by a spontaneous tail tubular mutation

Bacteriophage-resistant carbapenem-resistant Klebsiella pneumoniae shows reduced antibiotic resistance and virulence

Clinical and laboratory insights into the threat of hypervirulent Klebsiella pneumoniae

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