細胞外膜蛋白 C 為革蘭氏陰性菌上主要的通道蛋白之一，其作用是作為細胞膜之滲透管道，在大腸桿菌中為養分及抗生素之重要通過管道。本研究主要目的為探討細胞外膜蛋白 C 抗體於小鼠模式中對於野生菌株及細胞外膜蛋白 C 變異之大腸桿菌感染上所扮演的角色。將純化後的細胞外膜蛋白 C 蛋白質與佛朗氏佐劑混和後打入六週大小鼠腹腔內，抗體之效價於第四週時被偵測 ; 並在第五週時，將老鼠分別感染五倍致死劑量之野生菌株及細胞外膜蛋白 C 變異之大腸桿菌，並計算老鼠存活率。結果顯示細胞外膜蛋白 C 抗體可提高老鼠對於感染之抵抗力，同時也可保護小鼠對抗細胞外膜蛋白 C 變異菌株之感染。利用間接免疫螢光染色及西方墨點法證實細胞外膜蛋白 C 抗體可辨識到細胞外膜蛋白 C 變異之大腸桿菌，暗示此抗體有非特異性交叉反應。比較細胞外膜蛋白 C 之胺基酸序列及大腸桿菌全基因後，發現其胺基酸序列和細胞外膜磷化蛋白 E 及細胞外膜蛋白 A 存在高度相似性。藉由合成對細胞外膜蛋白 C 外露環狀結構之胜肽並在小鼠中生產其抗體，發現在小鼠模式中對於野生菌株及細胞外膜蛋白 C 變異之菌株還是存在抗體交叉反應的現象。在 K-12 大腸桿菌上突變三種主要細胞外膜蛋白，包括細胞外膜蛋白 C 、細胞外膜蛋白 A 以及細胞外膜蛋白 F ，得到七種單一、雙重及多重細胞外膜蛋白變異之 K-12 大腸桿菌。利用西方墨點法證實細胞外膜蛋白 C 抗體對於 K-12 大腸桿菌細胞外膜蛋白 A 仍具有抗體交叉反應，但在細胞外膜蛋白 F 上並無此反應。這些結果顯示著，在小鼠模式中，由於細胞外膜蛋白 C 抗體對於細胞外膜蛋白 A 具有抗體交叉反應，可以保護大腸桿菌野生株及細胞外膜蛋白 C 變異菌株之感染。這也暗示著，細胞外膜蛋白 C 可作為良好的免疫源以產生具有交叉反應之抗體，用以對抗大腸桿菌之感染。

Outer membrane protein C (OmpC), one of the major porins located on Gram-negative bacteria, serves as the permeability channel in Escherichia coli to uptake nutrients and antibiotics. The objective of this study is to demonstrate the in vivo evidence to show the protection of anti-OmpC antibody against the infection of OmpC-expressed and OmpC-deficient E. coli. Recombinant OmpC protein combined with Freund’s adjuvant was injected into mice. After five weeks of injection, mice were challenged with OmpC-expressed E. coli and ompC mutant. The results showed that most of the mice without anti-OmpC antibody were died from serious infection, but OmpC-immunized mice had higher survival rate. Nevertheless, the protective efficacy of anti-OmpC antibody against OmpC-expressed E. coli and ompC mutants had no significant differences in the number of survived mice. Both indirect immunofluorescence assay and western blot showed ompC mutant could be recognized by anti-OmpC antibody. Comparing the OmpC amino acid sequence with E. coli whole genome, I found that OmpC has high similarity with other porins including outer membrane protein A (OmpA) and outer membrane phosphoporin protein E (PhoE). Synthesized peptides that specific for OmpC loop region were used to minimize the effect of OmpA and PhoE cross-immunity, but the data showed anti-peptide antibody still had the cross-reactivity with other porins on E. coli. Seven porin mutants of E. coli K-12 strain were constructed, including single, double and triple porin mutation of ompC, ompA, and ompF. SDS-PAGE and western blotting showed anti-OmpC antibody cross-reacted with E. coli K-12 OmpA but not OmpF. In conclusion, these data indicate that by the cross-reactivity of anti-OmpC antibody against OmpA, anti-OmpC antibody protected the mice from the infection of wild-type E. coli and ompC mutant. Therefore, OmpC can be a good vaccine candidate to generate polyclonal antibody for the protection of E. coli infection in the future.

Adler, M., Anjum, M., Andersson, D.I., and Sandegren, L. (2013). Influence of acquired beta-lactamases on the evolution of spontaneous carbapenem resistance in Escherichia coli. The Journal of Antimicrobial Chemotherapy 68, 51-59.
Alcantar-Curiel, M.D., Garcia-Latorre, E., and Santos, J.I. (2000). Klebsiella pneumoniae 35 and 36 kDa porins are common antigens in different serotypes and induce opsonizing antibodies. Archives of Medical Research 31, 28-36.
Armand-Lefevre, L., Leflon-Guibout, V., Bredin, J., Barguellil, F., Amor, A., Pages, J.M., and Nicolas-Chanoine, M.H. (2003). Imipenem resistance in Salmonella enterica serovar Wien related to porin loss and CMY-4 beta-lactamase production. Antimicrobial Agents and Chemotherapy 47, 1165-1168.
Arnott, I.D., Landers, C.J., Nimmo, E.J., Drummond, H.E., Smith, B.K., Targan, S.R., and Satsangi, J. (2004). Sero-reactivity to microbial components in Crohn's disease is associated with disease severity and progression, but not NOD2/CARD15 genotype. The American Journal of Gastroenterology 99, 2376-2384.
Basle, A., Rummel, G., Storici, P., Rosenbusch, J.P., and Schirmer, T. (2006). Crystal structure of osmoporin OmpC from E. coli at 2.0 A. Journal of Molecular Biology 362, 933-942.
Batchelor, E., Walthers, D., Kenney, L.J., and Goulian, M. (2005). The Escherichia coli CpxA-CpxR envelope stress response system regulates expression of the porins ompF and ompC. Journal of Bacteriology 187, 5723-5731.
Bauer, K., Struyve, M., Bosch, D., Benz, R., and Tommassen, J. (1989). One single lysine residue is responsible for the special interaction between polyphosphate and the outer membrane porin PhoE of Escherichia coli. The Journal of Biological Chemistry 264, 16393-16398.
Benjamin, D.C., and Perdue, S.S. (1996). Site-directed mutagenesis in epitope mapping. Methods 9, 508-515.
Benz, R., and Bauer, K. (1988). Permeation of hydrophilic molecules through the outer membrane of gram-negative bacteria. Review on bacterial porins. European Journal of Biochemistry / FEBS 176, 1-19.
Bishayee, S., Majumdar, S., Scher, C.D., and Khan, S. (1988). Characterization of a novel anti-peptide antibody that recognizes a specific conformation of the platelet-derived growth factor receptor. Molecular and Cellular Biology 8, 3696-3702.
Blattner, F.R., Plunkett, G., 3rd, Bloch, C.A., Perna, N.T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J.D., Rode, C.K., Mayhew, G.F., et al. (1997). The complete genome sequence of Escherichia coli K-12. Science 277, 1453-1462.
Chai, T.J., and Foulds, J. (1977). Purification of protein A, an outer membrane component missing in Escherichia coli K-12 ompA mutants. Biochimica et Biophysica acta 493, 210-215.
Chen, S., Zhang, A., Blyn, L.B., and Storz, G. (2004). MicC, a second small-RNA regulator of Omp protein expression in Escherichia coli. Journal of Bacteriology 186, 6689-6697.
Confer, A.W., and Ayalew, S. (2013). The OmpA family of proteins: roles in bacterial pathogenesis and immunity. Veterinary Microbiology 163, 207-222.
Cowan, S.W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R.A., Jansonius, J.N., and Rosenbusch, J.P. (1992). Crystal structures explain functional properties of two E. coli porins. Nature 358, 727-733.
Croxen, M.A., and Finlay, B.B. (2010). Molecular mechanisms of Escherichia coli pathogenicity. Nature Reviews Microbiology 8, 26-38.
Dabo, S.M., Confer, A., Montelongo, M., York, P., and Wyckoff, J.H. 3rd,. (2008). Vaccination with Pasteurella multocida recombinant OmpA induces strong but non-protective and deleterious Th2-type immune response in mice. Vaccine 26, 4345-4351.
Datsenko, K.A., and Wanner, B.L. (2000). One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proceedings of the National Academy of Sciences of the United States of America 97, 6640-6645.
Delcour, A.H. (2003). Solute uptake through general porins. Frontiers in Bioscience 8, d1055-1071.
Dumetz, F., Lapatra, S.E., Duchaud, E., Claverol, S., and Le Henaff, M. (2007). The Flavobacterium psychrophilum OmpA, an outer membrane glycoprotein, induces a humoral response in rainbow trout. Journal of Applied Microbiology 103, 1461-1470.
Ferrario, M., Ernsting, B.R., Borst, D.W., Wiese, D.E., 2nd, Blumenthal, R.M., and Matthews, R.G. (1995). The leucine-responsive regulatory protein of Escherichia coli negatively regulates transcription of ompC and micF and positively regulates translation of ompF. Journal of Bacteriology 177, 103-113.
Findlay, J., Hamouda, A., Dancer, S.J., and Amyes, S.G. (2012). Rapid acquisition of decreased carbapenem susceptibility in a strain of Klebsiella pneumoniae arising during meropenem therapy. Clinical Microbiology and Infection 18, 140-146.
Foulds, J., and Chai, T.J. (1978). Defeat of colicin tolerance in Escherichia coli ompA mutants: evidence for interaction between colicin L-JF246 and the cytoplasmic membrane. Journal of Bacteriology 133, 158-164.
Frank, S.A. (2002). In Immunology and Evolution of Infectious Disease (Princeton (NJ)). Page 70.
Gophna, U., Ideses, D., Rosen, R., Grundland, A., and Ron, E.Z. (2004). OmpA of a septicemic Escherichia coli O78--secretion and convergent evolution. International Journal of Medical Microbiology 294, 373-381.
Guillier, M., Gottesman, S., and Storz, G. (2006). Modulating the outer membrane with small RNAs. Genes & Development 20, 2338-2348.
Hagge, S.O., de Cock, H., Gutsmann, T., Beckers, F., Seydel, U., and Wiese, A. (2002). Pore formation and function of phosphoporin PhoE of Escherichia coli are determined by the core sugar moiety of lipopolysaccharide. The Journal of Biological Chemistry 277, 34247-34253.
Hong, H., Szabo, G., and Tamm, L.K. (2006). Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening. Nature Chemical Biology 2, 627-635.
Ish-Horowicz, D., and Burke, J.F. (1981). Rapid and efficient cosmid cloning. Nucleic Acids Research 9, 2989-2998.
Jarzab, A., Witkowska, D., Ziomek, E., Dabrowska, A., Szewczuk, Z., and Gamian, A. (2013). Shigella flexneri 3a Outer membrane protein C epitope is recognized by human umbilical cord sera and associated with protective activity. PLoS One 8, e70539.
Kaeriyama, M., Machida, K., Kitakaze, A., Wang, H., Lao, Q., Fukamachi, T., Saito, H., and Kobayashi, H. (2006). OmpC and OmpF are required for growth under hyperosmotic stress above pH 8 in Escherichia coli. Letters in Applied Microbiology 42, 195-201.
Kaper, J.B., Nataro, J.P., and Mobley, H.L. (2004). Pathogenic Escherichia coli. Nature Reviews Microbiology 2, 123-140.
Keitel, T., Kramer, A., Wessner, H., Scholz, C., Schneider-Mergener, J., and Hohne, W. (1997). Crystallographic analysis of anti-p24 (HIV-1) monoclonal antibody cross-reactivity and polyspecificity. Cell 91, 811-820.
Koebnik, R. (1999). Structural and functional roles of the surface-exposed loops of the beta-barrel membrane protein OmpA from Escherichia coli. Journal of Bacteriology 181, 3688-3694.
Koebnik, R., Locher, K.P., and Van Gelder, P. (2000). Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Molecular Microbiology 37, 239-253.
Kohanski, M.A., Dwyer, D.J., Hayete, B., Lawrence, C.A., and Collins, J.J. (2007). A common mechanism of cellular death induced by bactericidal antibiotics. Cell 130, 797-810.
Koizumi, N., and Watanabe, H. (2003). Molecular cloning and characterization of a novel leptospiral lipoprotein with OmpA domain. FEMS Microbiology Letters 226, 215-219.
Kosek, M., Bern, C., and Guerrant, R.L. (2003). The global burden of diarrhoeal disease, as estimated from studies published between 1992 and 2000. Bulletin of the World Health Organization 81, 197-204.
Krishnan, S., and Prasadarao, N.V. (2012). Outer membrane protein A and OprF: versatile roles in Gram-negative bacterial infections. The FEBS Journal 279, 919-931.
Kumar, S., Kapil, S., Gautam, V., Verma, S.K., and Ray, P. (2010). Peptides representing the specific variable regions but not the full porin proteins can be useful for antibody based diagnosis of typhoid fever. Folia Microbiologica 55, 520-527.
Kung, C.H., Ku, W.W., Lee, C.H., Fung, C.P., Kuo, S.C., Chen, T.L., and Lee, Y.T. (2013). Epidemiology and risk factors of community-onset urinary tract infection caused by extended-spectrum beta-lactamase-producing Enterobacteriaceae in a medical center in Taiwan: A prospective cohort study. Journal of Microbiology, Immunology, and Infection. DOI : 10.1016/j.jmii.2013.08.006.
Landry, R.C., Klimowicz, A.C., Lavictoire, S.J., Borisova, S., Kottachchi, D.T., Lorimer, I.A., and Evans, S.V. (2001). Antibody recognition of a conformational epitope in a peptide antigen: Fv-peptide complex of an antibody fragment specific for the mutant EGF receptor, EGFRvIII. Journal of Molecular Biology 308, 883-893.
Lartigue, M.F., Poirel, L., Poyart, C., Reglier-Poupet, H., and Nordmann, P. (2007). Ertapenem resistance of Escherichia coli. Emerging Infectious Diseases 13, 315-317.
Lavoie, T.B., Mohan, S., Lipschultz, C.A., Grivel, J.C., Li, Y., Mainhart, C.R., Kam-Morgan, L.N., Drohan, W.N., and Smith-Gill, S.J. (1999). Structural differences among monoclonal antibodies with distinct fine specificities and kinetic properties. Molecular Immunology 36, 1189-1205.
Lescar, J., Pellegrini, M., Souchon, H., Tello, D., Poljak, R.J., Peterson, N., Greene, M., and Alzari, P.M. (1995). Crystal structure of a cross-reaction complex between Fab F9.13.7 and guinea fowl lysozyme. The Journal of Biological Chemistry 270, 18067-18076.
Li, H., Xiong, X.P., Peng, B., Xu, C.X., Ye, M.Z., Yang, T.C., Wang, S.Y., and Peng, X.X. (2009). Identification of broad cross-protective immunogens using heterogeneous antiserum-based immunoproteomic approach. Journal of Proteome Research 8, 4342-4349.
Lin, M.C., Chiu, N.C., Chi, H., Ho, C.S., and Huang, F.Y. (2013). Evolving trends of neonatal and childhood bacterial meningitis in northern Taiwan. Journal of Microbiology, Immunology, and Infection. DOI : 10.1016/j.jmii.2013.08.012.
Liu, C., Chen, Z., Tan, C., Liu, W., Xu, Z., Zhou, R., and Chen, H. (2012a). Immunogenic characterization of outer membrane porins OmpC and OmpF of porcine extraintestinal pathogenic Escherichia coli. FEMS Microbiology Letters 337, 104-111.
Liu, X., and Ferenci, T. (1998). Regulation of porin-mediated outer membrane permeability by nutrient limitation in Escherichia coli. Journal of Bacteriology 180, 3917-3922.
Liu, X., and Ferenci, T. (2001). An analysis of multifactorial influences on the transcriptional control of ompF and ompC porin expression under nutrient limitation. Microbiology 147, 2981-2989.
Liu, Y.F., Yan, J.J., Ko, W.C., Tsai, S.H., and Wu, J.J. (2008). Characterization of carbapenem-non-susceptible Escherichia coli isolates from a university hospital in Taiwan. The Journal of Antimicrobial Chemotherapy 61, 1020-1023.
Liu, Y.F., Yan, J.J., Lei, H.Y., Teng, C.H., Wang, M.C., Tseng, C.C., and Wu, J.J. (2012). Loss of outer membrane protein C in Escherichia coli contributes to both antibiotic resistance and escaping antibody-dependent bactericidal activity. Infection and Immunity 80, 1815-1822.
Lou, H., Chen, M., Black, S.S., Bushell, S.R., Ceccarelli, M., Mach, T., Beis, K., Low, A.S., Bamford, V.A., Booth, I.R., et al. (2011). Altered antibiotic transport in ompC mutants isolated from a series of clinical strains of multi-drug resistant E. coli. PLoS One 6, e25825.
Lukjancenko, O., Wassenaar, T.M., and Ussery, D.W. (2010). Comparison of 61 sequenced Escherichia coli genomes. Microbial Ecology 60, 708-720.
Manges, A.R., Johnson, J.R., Foxman, B., O'Bryan, T.T., Fullerton, K.E., and Riley, L.W. (2001). Widespread distribution of urinary tract infections caused by a multidrug-resistant Escherichia coli clonal group. The New England Journal of Medicine 345, 1007-1013.
Meyer-Hoffert, U., and Wiedow, O. (2011). Neutrophil serine proteases: mediators of innate immune responses. Current Opinion in Hematology 18, 19-24.
Molloy, M.P., Herbert, B.R., Slade, M.B., Rabilloud, T., Nouwens, A.S., Williams, K.L., and Gooley, A.A. (2000). Proteomic analysis of the Escherichia coli outer membrane. European Journal of Biochemistry. FEBS 267, 2871-2881.
Mow, W.S., Vasiliauskas, E.A., Lin, Y.C., Fleshner, P.R., Papadakis, K.A., Taylor, K.D., Landers, C.J., Abreu-Martin, M.T., Rotter, J.I., Yang, H., et al. (2004). Association of antibody responses to microbial antigens and complications of small bowel Crohn's disease. Gastroenterology 126, 414-424.
Nataro, J.P. (2005). Enteroaggregative Escherichia coli pathogenesis. Current Opinion in Gastroenterology 21, 4-8.
Nicholson, T.F., Watts, K.M., and Hunstad, D.A. (2009). OmpA of uropathogenic Escherichia coli promotes postinvasion pathogenesis of cystitis. Infection and Immunity 77, 5245-5251.
Nikaido, H. (2003). Molecular basis of bacterial outer membrane permeability revisited. Microbiology and Molecular Biology Reviews : 67, 593-656.
Oram, J.D., and Reiter, B. (1968). Inhibition of bacteria by lactoferrin and other iron-chelating agents. Biochimica et Biophysica Acta 170, 351-365.
Ortiz, V., Isibasi, A., Garcia-Ortigoza, E., and Kumate, J. (1989). Immunoblot detection of class-specific humoral immune response to outer membrane proteins isolated from Salmonella typhi in humans with typhoid fever. Journal of Clinical Microbiology 27, 1640-1645.
Overbeeke, N., Bergmans, H., van Mansfeld, F., and Lugtenberg, B. (1983). Complete nucleotide sequence of phoE, the structural gene for the phosphate limitation inducible outer membrane pore protein of Escherichia coli K12. Journal of Molecular Biology 163, 513-532.
Pages, J.M., James, C.E., and Winterhalter, M. (2008). The porin and the permeating antibiotic: a selective diffusion barrier in Gram-negative bacteria. Nature Reviews Microbiology 6, 893-903.
Papp, M., Altorjay, I., Norman, G.L., Shums, Z., Palatka, K., Vitalis, Z., Foldi, I., Lakos, G., Tumpek, J., Udvardy, M.L., et al. (2007). Seroreactivity to microbial components in Crohn's disease is associated with ileal involvement, noninflammatory disease behavior and NOD2/CARD15 genotype, but not with risk for surgery in a Hungarian cohort of IBD patients. Inflammatory Bowel Diseases 13, 984-992.
Pautsch, A., and Schulz, G.E. (2000). High-resolution structure of the OmpA membrane domain. Journal of Molecular Biology 298, 273-282.
Phale, P.S., Philippsen, A., Kiefhaber, T., Koebnik, R., Phale, V.P., Schirmer, T., and Rosenbusch, J.P. (1998). Stability of trimeric OmpF porin: the contributions of the latching loop L2. Biochemistry 37, 15663-15670.
Pinilla, C., Martin, R., Gran, B., Appel, J.R., Boggiano, C., Wilson, D.B., and Houghten, R.A. (1999). Exploring immunological specificity using synthetic peptide combinatorial libraries. Current Opinion in Immunology 11, 193-202.
Poirel, L., Heritier, C., Spicq, C., and Nordmann, P. (2004). In vivo acquisition of high-level resistance to imipenem in Escherichia coli. Journal of Clinical Microbiology 42, 3831-3833.
Pore, D., Mahata, N., Pal, A., and Chakrabarti, M.K. (2011). Outer membrane protein A (OmpA) of Shigella flexneri 2a, induces protective immune response in a mouse model. PloS One 6, e22663.
Prager, E.M. (1993). The sequence-immunology correlation revisited: data for cetacean myoglobins and mammalian lysozymes. Journal of Molecular Evolution 37, 408-416.
Prejit, Agarwal, R.K., Porteen, K., Dubal, Z.B., Asha, K., Shweta, S., and Ripan, B. (2013). Evaluation of recombinant outer membrane protein based vaccine against Salmonella Typhimurium in birds. Biologicals. Journal of the International Association of Biological Standardization 41, 162-168.
Richards, F.F., Konigsberg, W.H., Rosenstein, R.W., and Varga, J.M. (1975). On the specificity of antibodies. Science 187, 130-137.
Rodriguez-Morales, O., Fernandez-Mora, M., Hernandez-Lucas, I., Vazquez, A., Puente, J.L., and Calva, E. (2006). Salmonella enterica serovar Typhimurium ompS1 and ompS2 mutants are attenuated for virulence in mice. Infection and Immunity 74, 1398-1402.
Rolhion, N., Carvalho, F.A., and Darfeuille-Michaud, A. (2007). OmpC and the sigma (E) regulatory pathway are involved in adhesion and invasion of the Crohn's disease-associated Escherichia coli strain LF82. Molecular Microbiology 63, 1684-1700.
Salazar-Gonzalez, R.M., Maldonado-Bernal, C., Ramirez-Cruz, N.E., Rios-Sarabia, N., Beltran-Nava, J., Castanon-Gonzalez, J., Castillo-Torres, N., Palma-Aguirre, J.A., Carrera-Camargo, M., Lopez-Macias, C., et al. (2004). Induction of cellular immune response and anti-Salmonella enterica serovar typhi bactericidal antibodies in healthy volunteers by immunization with a vaccine candidate against typhoid fever. Immunology Letters 93, 115-122.
Sato, M., Machida, K., Arikado, E., Saito, H., Kakegawa, T., and Kobayashi, H. (2000). Expression of outer membrane proteins in Escherichia coli growing at acid pH. Applied and Environmental Microbiology 66, 943-947.
Schulz, G.E. (2002). The structure of bacterial outer membrane proteins. Biochimica et Biophysica Acta 1565, 308-317.
Schweizer, M., Hindennach, I., Garten, W., and Henning, U. (1978). Major proteins of the Escherichia coli outer cell envelope membrane. Interaction of protein II with lipopolysaccharide. European Journal of Biochemistry. FEBS 82, 211-217.
See, S.B., and Thomas, W.R. (2013). Protective anti-outer membrane protein immunity against Pasteurella pneumotropica infection of mice. Microbes and Infection 15, 470-479.
Singh, S.P., Williams, Y.U., Miller, S., and Nikaido, H. (2003). The C-terminal domain of Salmonella enterica serovar typhimurium OmpA is an immunodominant antigen in mice but appears to be only partially exposed on the bacterial cell surface. Infection and Immunity 71, 3937-3946.
Smith, S.G., Mahon, V., Lambert, M.A., and Fagan, R.P. (2007). A molecular Swiss army knife: OmpA structure, function and expression. FEMS Microbiology Letters 273, 1-11.
Soulas, C., Baussant, T., Aubry, J.P., Delneste, Y., Barillat, N., Caron, G., Renno, T., Bonnefoy, J.Y., and Jeannin, P. (2000). Outer membrane protein A (OmpA) binds to and activates human macrophages. Journal of Immunology 165, 2335-2340.
Su, L.H., Wu, T.L., and Chiu, C.H. (2012). Development of carbapenem resistance during therapy for non-typhoid Salmonella infection. Clinical Microbiology and Infection 18, E91-94.
Sundara Baalaji, N., Acharya, K.R., Singh, T.P., and Krishnaswamy, S. (2005). High-resolution diffraction from crystals of a membrane-protein complex: bacterial outer membrane protein OmpC complexed with the antibacterial eukaryotic protein lactoferrin. Structural Biology and Crystallization Communications 61, 773-775.
Thanavala, Y., and Lugade, A.A. (2011). Role of nontypeable Haemophilus influenzae in otitis media and chronic obstructive pulmonary disease. Advances in Oto-Rhino-Laryngology 72, 170-175.
Tifrea, D.F., Ralli-Jain, P., Pal, S., and de la Maza, L.M. (2013). Vaccination with the recombinant major outer membrane protein elicits antibodies to the constant domains and induces cross-serovar protection against intranasal challenge with Chlamydia trachomatis. Infection and Immunity 81, 1741-1750.
Ting, Y.T., Lu, C.Y., Shao, P.L., Lee, P.I., Chen, J.M., Hsueh, P.R., Huang, L.M., and Chang, L.Y. (2013). Epidemiology of community-acquired bacteremia among infants in a medical center in Taiwan, 2002-2011. Journal of Microbiology, Immunology, and Infection. DOI : 10.1016/j.jmii.2013.10.005.
Torres, A.G., Li, Y., Tutt, C.B., Xin, L., Eaves-Pyles, T., and Soong, L. (2006). Outer membrane protein A of Escherichia coli O157:H7 stimulates dendritic cell activation. Infection and Immunity 74, 2676-2685.
Van Gelder, P., Saint, N., van Boxtel, R., Rosenbusch, J.P., and Tommassen, J. (1997). Pore functioning of outer membrane protein PhoE of Escherichia coli: mutagenesis of the constriction loop L3. Protein Engineering 10, 699-706.
Van Regenmortel, M.H. (1998). From absolute to exquisite specificity. Reflections on the fuzzy nature of species, specificity and antigenic sites. Journal of Immunological Methods 216, 37-48.
Vermont, C.L., van Dijken, H.H., Kuipers, A.J., van Limpt, C.J., Keijzers, W.C., van der Ende, A., de Groot, R., van Alphen, L., and van den Dobbelsteen, G.P. (2003). Cross-reactivity of antibodies against PorA after vaccination with a meningococcal B outer membrane vesicle vaccine. Infection and Immunity 71, 1650-1655.
Wang, Y. (2002). The function of OmpA in Escherichia coli. Biochemical and Biophysical Research Communications 292, 396-401.
Wattam, A.R., Abraham, D., Dalay, O., Disz, T.L., Driscoll, T., Gabbard, J.L., Gillespie, J.J., Gough, R., Hix, D., Kenyon, R., et al. (2014). PATRIC, the bacterial bioinformatics database and analysis resource. Nucleic Acids Research 42, D581-591.
Wirth, T., Falush, D., Lan, R., Colles, F., Mensa, P., Wieler, L.H., Karch, H., Reeves, P.R., Maiden, M.C., Ochman, H., et al. (2006). Sex and virulence in Escherichia coli: an evolutionary perspective. Molecular Microbiology 60, 1136-1151.
Witkowska, D., Czarny, A., and Mulczyk, M. (1986). Humoral response in mice immunized with outer membrane proteins of Shigella flexneri. Archivum Immunologiae et Therapiae Experimentalis 34, 499-504.
Witkowska, D., Czarny, A., and Mulczyk, M. (1992). Humoral response in mice immunized with outer membrane proteins of Hafnia alvei. Protective activity of anti-OMP-antibodies. Archivum Immunologiae et Therapiae Experimentalis 40, 301-304.
Witkowska, D., Mleczko, J., and Mulczyk, M. (1985). Transfer of immunity by means of spleen cells from mice immunized with outer membrane proteins of Shigella flexneri. Archivum Immunologiae et Therapiae Experimentalis 33, 629-635.
Wu, H.H., Yang, Y.Y., Hsieh, W.S., Lee, C.H., Leu, S.J., and Chen, M.R. (2009). OmpA is the critical component for Escherichia coli invasion-induced astrocyte activation. Journal of Neuropathology and Experimental Neurology 68, 677-690.
Wu, J.H., Chiou, Y.H., Chang, J.T., Wang, H.P., Chen, Y.Y., and Hsieh, K.S. (2012). Urinary tract infection in infants: a single-center clinical analysis in southern Taiwan. Pediatrics and Neonatology 53, 283-288.
Wu, J.J., Wang, L.R., Liu, Y.F., Chen, H.M., and Yan, J.J. (2011). Prevalence and characteristics of ertapenem-resistant Klebsiella pneumoniae isolates in a Taiwanese university hospital. Microbial Drug Resistance 17, 259-266.
Yan, J.J., Wu, J.J., Lee, C.C., Ko, W.C., and Yang, F.C. (2010). Prevalence and characteristics of ertapenem-nonsusceptible Escherichia coli in a Taiwanese university hospital, 1999 to 2007. European Journal of Clinical Microbiology & Infectious Diseases 29, 1417-1425.
Yoshida, T., Qin, L., Egger, L.A., and Inouye, M. (2006). Transcription regulation of ompF and ompC by a single transcription factor, OmpR. The Journal of Biological Chemistry 281, 17114-17123.
Zholudev, A., Zurakowski, D., Young, W., Leichtner, A., and Bousvaros, A. (2004). Serologic testing with ANCA, ASCA, and anti-OmpC in children and young adults with Crohn's disease and ulcerative colitis: diagnostic value and correlation with disease phenotype. The American Journal of Gastroenterology 99, 2235-2241.