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  • Chu, Yuefeng  (3)
  • Biodiversity Research  (3)
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  • Biodiversity Research  (3)
  • 1
    In: The FASEB Journal, Wiley, Vol. 37, No. 10 ( 2023-10)
    Abstract: Mycoplasma spp., the smallest self‐replicating and genome‐reduced organisms, have raised a great concern in both the medical and veterinary fields due to their pathogenicity. The molecular determinants of these wall‐less bacterium efficiently use their limited genes to ensure successful infection of the host remain unclear. In the present study, we used the ruminant pathogen Mycoplasma bovis as a model to identify the key factors for colonization and invasion into host cells. We constructed a nonredundant fluorescent transposon mutant library of M. bovis using a modified transposon plasmid, and identified 34 novel adhesion‐related genes based on a high‐throughput screening approach. Among them, the Δ LppB mutant exhibited the most apparent decrease in adhesion to embryonic bovine lung (EBL) cells. The surface‐localized lipoprotein LppB, which is highly conserved in Mycoplasma species, was then confirmed as a key factor for M. bovis adhesion with great immunogenicity. LppB interacted with various components (fibronectin, vitronectin, collagen IV, and laminin) of host extracellular matrix (ECM) and promoted plasminogen activation through tPA to degrade ECM. The 439–502 amino acid region of LppB is a critical domain, and F465 and Y493 are important residues for the plasminogen activation activity. We further revealed LppB as a key factor facilitating internalization through clathrin‐ and lipid raft‐mediated endocytosis, which helps the Mycoplasma invade the host cells. Our study indicates that LppB plays a key role in Mycoplasma infection and is a potential new therapeutic and vaccine target for Mycoplasma species.
    Type of Medium: Online Resource
    ISSN: 0892-6638 , 1530-6860
    URL: Issue
    Language: English
    Publisher: Wiley
    Publication Date: 2023
    detail.hit.zdb_id: 1468876-1
    SSG: 12
    Location Call Number Limitation Availability
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  • 2
    In: Journal of Basic Microbiology, Wiley, Vol. 61, No. 2 ( 2021-02), p. 133-146
    Abstract: Five annotated genomes of Mycoplasma hyorhinis were analyzed for clarifying evolutionary dynamics driving the overall codon usage pattern. Information entropy used for estimating nucleotide usage pattern at the gene level indicates that multiple evolutionary dynamics participate in forcing nucleotide usage bias at every codon position. Moreover, nucleotide usage bias directly contributes to synonymous codon usage biases with two different extremes. The overrepresented codons tended to have A/T in the third codon position, and the underrepresented codons strongly used G/C in the third position. Furthermore, correspondence analysis and neutrality plot reflect an obvious interplay between mutation pressure and natural selection mediating codon usage in M. hyorhinis genome. Due to significant bias in usages between A/T and G/C at the gene level, different selective forces have been proposed to contribute to codon usage preference in M. hyorhinis genome, including nucleotide composition constraint derived from mutation pressure, translational selection involved in natural selection, and strand‐specific mutational bias represented by different nucleotide skew index. The systemic analyses of codon usage for M. hyorhinis can enable us to better understand the mechanisms of evolution in this species.
    Type of Medium: Online Resource
    ISSN: 0233-111X , 1521-4028
    URL: Issue
    Language: English
    Publisher: Wiley
    Publication Date: 2021
    detail.hit.zdb_id: 1480967-9
    detail.hit.zdb_id: 632513-0
    detail.hit.zdb_id: 203025-1
    SSG: 12
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  • 3
    In: The FASEB Journal, Wiley, Vol. 37, No. 5 ( 2023-05)
    Abstract: Colistin (polymyxin E) is a group of cationic antimicrobial cyclic peptides and is recognized as a last‐resort defense against lethal infections with carbapenem‐resistant pathogens. In addition to the plasmid‐borne mobilized phosphoethanolamine (PEA) transferases, the functional expression of lipid A‐modifying enzymes encoded on chromosomes has been attributed to intrinsic bacterial colistin resistance. However, the mechanisms of colistin resistance in Riemerella anatipestifer remain unknown. Herein, the GE296_RS09715 gene‐encoded Lipid A PEA transferases (RaEptA) was identified in R. anatipestifer . Genetic and structural analyses revealed that the amino acid sequence of RaEptA shared 26.6%–33.1% similarities with the family of Lipid A PEA transferases (EptA) and MCR‐like proteins and have defined 12 residues that contribute to the formation of phosphatidylethanolamine (PE)‐recognizable cavities. Comparative analyses of colistin resistance in RA‐LZ01 and RA‐LZ01ΔRaEptA showed the level of colistin has fallen from 96 μg mL −1 down to 24 ~ 32 μg mL −1 . Site‐directed mutagenesis assay of the PE‐binding cavity and expression of the mutants reveals that K309‐rRaEptA can remodel the surface of Escherichia coli and rendering it resistant to colistin, suggesting this point‐mutation of P309K is necessary for EptA‐mediated lipid A modification. Moreover, the virulence of RA‐LZ01ΔRaEptA was attenuated compared with RA‐LZ01 both in vivo and vitro. Taken together, the results represent the RaEptA involved in the colistin resistance and pathogenicity, and the P309K mutation might alter bacterial adaptation and increase the spread of colistin resistance from R. anatipestifer to other gram‐negative bacteria. The findings of this study suggest another scenario for the spread of colistin resistance genes and should be considered by a wide audience.
    Type of Medium: Online Resource
    ISSN: 0892-6638 , 1530-6860
    URL: Issue
    Language: English
    Publisher: Wiley
    Publication Date: 2023
    detail.hit.zdb_id: 1468876-1
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
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