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. 2020 Oct 6;11:589234. doi: 10.3389/fmicb.2020.589234

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Copyright © 2020 Uppalapati, Sett and Pathania.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Function of major OMPs in A. baumannii. Five major OMPs with their substrate specificity is shown. OmpA porin mediates uptake of β-lactam and colistin antibiotics. Human antimicrobial peptide LL-37 and bovine AMP BMAP-28 may bind to the porin. OmpA pore size is optimal for uptake of iron siderophores like acenitobactin. A coiled loop in the C-terminal region of the protein binds to peptidoglycan maintaining the membrane integrity. Phagocytosed A. baumannii releases OmpA into the cytoplasm of host cells. Secreted OmpA inhibits lysosome fusion to autophagosomes, enters into mitochondria inducing ROS generation. Secreted OmpA actively localizes to nucleus via nuclear pore complex where it activates apoptotic markers like caspases. Ab, A. baumannii; OM, outer membrane; PG, peptidoglycan; IM, inner membrane; sOmpA, secreted OmpA; ROS, reactive oxygen species.