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Napier, B. A. et al. Clinical use of colistin induces cross-resistance to host antimicrobials in Acinetobacter baumannii.
2. Napier BA, Burd EM, Satola SW, et al. Clinical use of colistin induces cross-resistance to host antimicrobials in Acinetobacter baumannii.
Thus, we sought to determine whether the antimicrobial δ-toxin, also known as PSMγ, produced by the resident cutaneous microbe, S. epidermidis, could interact with the host antimicrobials leading to greater pathogen inhibition and enhancement of the host's innate immune system.
Additionally, due to cross resistance between polymyxins and host antimicrobials (Band and Weiss, 2014), exposure to host cationic antimicrobial peptides may provide selective pressure for drug-resistant mutants to arise as soon as a bacterial infection is established and long before antibiotic therapy is even started.
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Collectively, our findings suggest that RfBPI/LBP plays an essential role in host antimicrobial defense, plausibly through selective eradication of invading bacteria.
Bactericidal permeability-increasing protein (BPI /lipopolysaccharide (LPS) binding proteins (LBPs) are well-known proteins that play an indispensable role in host antimicrobial defense.
To investigate whether adrenomedullin (ADM), a multifunctional peptide with key roles in host antimicrobial defence and inflammation, was present and quantifiable in human gingival crevicular fluid (GCF) and to study its relationship with periodontal health and disease.
Germline-encoded pattern recognition receptors (PRRs), like Toll-like receptors (TLRs), RIG-I-like receptors (RLRs) and NOD-like receptors (NLRs), recognize conserved molecular structures known as pathogen-associated molecular patterns (PAMPs) and initiate host antimicrobial response such as the production of type I interferons and other cytokines (Takeuchi and Akira, 2010).
To defend itself from the host antimicrobial agents, S. Typhimurium uses SPI2 effector proteins [27], [28].
Coimmunoprecipitation and tryptophan spectroscopy demonstrated direct binding of δ-toxin to host antimicrobial peptides LL-37, CRAMP, hBD2, and hBD3.
SE attaches to foreign material, interacts with the host extracellular matrix and elaborates biofilm, reducing deposition of complement/IgG, susceptibility to host antimicrobial peptides and neutrophil-mediated killing [3], [7], [8].
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