Page 115 - MI-2-4

Microbes & Immunity Brachyspira pilosicoli novel outer membrane proteins

the outer membrane lipoprotein and other major outer doi: 10.1371/journal.pbio.1001242
membrane proteins. J Bacteriol. 1978;136(1):280-285.
119. Biswas S, Mohammad MM, Movileanu L, Van Den Berg B.
doi: 10.1128/jb.136.1.280-285.1978 Crystal structure of the outer membrane protein OpdK from
Pseudomonas aeruginosa. Structure. 2008;16(7):1027-1035.
108. Sugawara E, Nikaido H. Pore-forming activity of OmpA
protein of Escherichia coli. J Biol Chem. 1992;267(4):2507-2511. doi: 10.1016/j.str.2008.04.009
doi: 10.1016/S0021-9258(18)45908-X 120. Kuehne SA, Cartman ST, Heap JT, Kelly ML, Cockayne A,
Minton NP. The role of toxin A and toxin B in Clostridium
109. Krishnan S, Prasadarao NV. Outer membrane protein A and difficile infection. Nature. 2010;467(7316):711-713.
OprF: Versatile roles in gram-negative bacterial infections.
FEBS J. 2012;279(6):919-931. doi: 10.1038/nature09397
doi: 10.1111/j.1742-4658.2012.08482.x 121. Van Den Berg B, Prathyusha Bhamidimarri S, Dahyabhai
Prajapati J, Kleinekathöfer U, Winterhalter M. Outer-
110. Laguri C, Sperandeo P, Pounot K, et al. Interaction of membrane translocation of bulky small molecules by passive
lipopolysaccharides at intermolecular sites of the periplasmic diffusion. Proc Natl Acad Sci. 2015;112(23):E2991-E2999.
Lpt transport assembly. Sci Rep. 2017;7(1):9715.
doi: 10.1073/pnas.1424835112
doi: 10.1038/s41598-017-10136-0
122. Pajatsch M, Andersen C, Mathes A, Böck A, Benz R,
111. Pieńko T, Trylska J. Extracellular loops of BtuB facilitate Engelhardt H. Properties of a cyclodextrin-specific,
transport of vitamin B12 through the outer membrane of E. unusual porin from Klebsiella oxytoca. J Biol Chem.
Coli. PLoS Comput Biol. 2020;16(7):e1008024. 1999;274(35):25159-25166.
doi: 10.1371/journal.pcbi.1008024 doi: 10.1074/jbc.274.35.25159
112. Di Girolamo PM, Kadner RJ, Bradbeer C. Isolation 123. Gruss F, Zähringer F, Jakob RP, Burmann BM, Hiller S,
of vitamin B 12 transport mutants of Escherichia coli. Maier T. The structural basis of autotransporter translocation
J Bacteriol. 1971;106(3):751-757. by TamA. Nat Struct Mol Biol. 2013;20(11):1318-1320.
doi: 10.1128/jb.106.3.751-757.1971 doi: 10.1038/nsmb.2689
113. White JC, Di Girolamo PM, Fu ML, Preston YA, Bradbeer 124. Selkrig J, Mosbahi K, Webb CT, et al. Discovery of an
C. Transport of vitamin B 12 in Escherichia coli. Location archetypal protein transport system in bacterial outer
and properties of the initial B 12 -binding site. J Biol Chem. membranes. Nat Struct Mol Biol. 2012;19(5):506-510.
1973;248(11):3978-3986.
doi: 10.1038/nsmb.2261
doi: 10.1016/S0021-9258(19)43828-3
125. Pavlova O, Peterson JH, Ieva R, Bernstein HD.
114. Noinaj N, Guillier M, Barnard TJ, Buchanan SK. TonB- Mechanistic link between β barrel assembly and the
dependent transporters: Regulation, structure, and function. initiation of autotransporter secretion. Proc Natl Acad Sci.
Annu Rev Microbiol. 2010;64(1):43-60. 2013;110(10):E938-E947.

doi: 10.1146/annurev.micro.112408.134247 doi: 10.1073/pnas.1219076110
115. Schauer K, Rodionov DA, De Reuse H. New substrates for 126. Matthijs S, Koedam N, Cornelis P, De Greve H. The
TonB-dependent transport: Do we only see the ‘tip of the trehalose operon of Pseudomonas fluorescens ATCC 17400.
iceberg’? Trends Biochem Sci. 2008;33(7):330-338. Res Microbiol. 2000;151(10):845-851.
doi: 10.1016/j.tibs.2008.04.012 doi: 10.1016/S0923-2508(00)01151-7
116. Biswas S, Mohammad MM, Patel DR, Movileanu L, Van Den 127. Abergel C, Bouveret E, Claverie JM, et al. Structure of the
Berg B. Structural insight into OprD substrate specificity. Escherichia coli TolB protein determined by MAD methods
Nat Struct Mol Biol. 2007;14(11):1108-1109. at 1.95 Å resolution. Structure. 1999;7(10):1291-1300.
doi: 10.1038/nsmb1304 doi: 10.1016/S0969-2126(00)80062-3
117. Moraes TF, Bains M, Hancock RE, Strynadka NC. An 128. Rigal A, Bouveret E, Lloubes R, Lazdunski C, Benedetti H.
arginine ladder in OprP mediates phosphate-specific The TolB protein interacts with the porins of Escherichia coli.
transfer across the outer membrane. Nat Struct Mol Biol. J Bacteriol. 1997;179(23):7274-7279.
2007;14(1):85-87.
doi: 10.1128/jb.179.23.7274-7279.1997
doi: 10.1038/nsmb1189
129. Fognini-Lefebvre N, Lazzaroni JC, Portalier R. tolA, tolB and
118. Eren E, Vijayaraghavan J, Liu J, et al. Substrate specificity excC, three cistrons involved in the control of pleiotropic
within a family of outer membrane carboxylate channels. release of periplasmic proteins by Escherichia coli K12. Mol
PLoS Biol. 2012;10(1):e1001242. Gen Genet. 1987;209:391-395.

Volume 2 Issue 4 (2025) 107 doi: 10.36922/MI025230050