TY - JOUR
T1 - Host–bacterial interactions
T2 - Outcomes of antimicrobial peptide applications
AU - Alkatheri, Asma Hussain
AU - Yap, Polly Soo-Xi
AU - Abushelaibi, Aisha
AU - Lai, Kok-Song
AU - Cheng, Wan-Hee
AU - Lim, Swee-Hua Erin
N1 - Funding Information:
This work was funded by the Interdisciplinary Research Grant from the Higher Colleges of Technology (Interdisciplinary_212322). The authors are grateful to Mariam Hussain Alkatheri for her support in designing the figures.
Publisher Copyright:
© 2022 by the authors.
PY - 2022/7
Y1 - 2022/7
N2 - The bacterial membrane is part of a secretion system which plays an integral role to secrete proteins responsible for cell viability and pathogenicity; pathogenic bacteria, for example, secrete virulence factors and other membrane-associated proteins to invade the host cells through various types of secretion systems (Type I to Type IX). The bacterial membrane can also mediate microbial communities’ communication through quorum sensing (QS), by secreting auto-stimulants to coordinate gene expression. QS plays an important role in regulating various physiological processes, including bacterial biofilm formation while providing increased virulence, subsequently leading to antimicrobial resistance. Multi-drug resistant (MDR) bacteria have emerged as a threat to global health, and various strategies targeting QS and biofilm formation have been explored by researchers worldwide. Since the bacterial secretion systems play such a crucial role in host–bacterial interactions, this review intends to outline current understanding of bacterial membrane systems, which may provide new insights for designing approaches aimed at antimicrobials discovery. Various mechanisms pertaining interaction of the bacterial membrane with host cells and antimicrobial agents will be highlighted, as well as the evolution of bacterial membranes in evasion of antimicrobial agents. Finally, the use of antimicrobial peptides (AMPs) as a cellular device for bacterial secretion systems will be discussed as emerging potential candidates for the treatment of multidrug resistance infections.
AB - The bacterial membrane is part of a secretion system which plays an integral role to secrete proteins responsible for cell viability and pathogenicity; pathogenic bacteria, for example, secrete virulence factors and other membrane-associated proteins to invade the host cells through various types of secretion systems (Type I to Type IX). The bacterial membrane can also mediate microbial communities’ communication through quorum sensing (QS), by secreting auto-stimulants to coordinate gene expression. QS plays an important role in regulating various physiological processes, including bacterial biofilm formation while providing increased virulence, subsequently leading to antimicrobial resistance. Multi-drug resistant (MDR) bacteria have emerged as a threat to global health, and various strategies targeting QS and biofilm formation have been explored by researchers worldwide. Since the bacterial secretion systems play such a crucial role in host–bacterial interactions, this review intends to outline current understanding of bacterial membrane systems, which may provide new insights for designing approaches aimed at antimicrobials discovery. Various mechanisms pertaining interaction of the bacterial membrane with host cells and antimicrobial agents will be highlighted, as well as the evolution of bacterial membranes in evasion of antimicrobial agents. Finally, the use of antimicrobial peptides (AMPs) as a cellular device for bacterial secretion systems will be discussed as emerging potential candidates for the treatment of multidrug resistance infections.
KW - antimicrobial peptides
KW - antimicrobial resistance
KW - bacterial membrane
KW - quorum sensing
KW - secreting system
UR - http://www.scopus.com/inward/record.url?scp=85136175778&partnerID=8YFLogxK
U2 - 10.3390/membranes12070715
DO - 10.3390/membranes12070715
M3 - Review Article
C2 - 35877918
AN - SCOPUS:85136175778
VL - 12
JO - Membranes
JF - Membranes
SN - 2077-0375
IS - 7
M1 - 715
ER -