Beck, Z., Matyas, G.R., Jalah, R., Rao, M., Polonis, V.R., Alving, C.R. (2015) Differential immune responses to HIV-1
envelope protein induced by liposomal adjuvant formulations containing monophosphoryl lipid A with or without
QS21. Vaccine 33:5578–5587.
Blake, M.S., Wetzler, L.M. (1995) Vaccines for gonorrhea: where are we on the curve? Trends Microbiol. 3:469–474.
Blankson, H., Stakkestad, J.A., Fagertun, H., Thom, E., Wadstein, J., Gudmundsen, O. (2000) Conjugated linoleic acid
reduces body fat mass in overweight and obese humans. J. Nutr. 130:2943–2948.
Bobbala, S., Hook, S. (2016) Is there an optimal formulation and delivery strategy for subunit vaccines? Pharm. Res.
33:2078–2097.
Brunham, R.C., Rey-Ladino, J. (2005) Immunology of Chlamydia infection: implications for a Chlamydia trachomatis
vaccine. Nature Rev. Immunol. 5:149–161.
Cai, S., He, F., Samra, H.S., de la Maza, L.M., Bottazzi, M., Joshi, S.B., Middaugh, C.R. (2009) Biophysical and
stabilization studies of the Chlamydia trachomatis mouse pneumonitis major outer membrane protein. Mol. Pharm.
6:1553–1561.
Brunham, R.C., Pourbohloul, B., Mak, S., White, R., Rekart, M.L. (2005) The unexpected impact of a Chlamydia
trachomatis infection control program on susceptibility to reinfection. J. Infect. Dis. 192:1836–1844.
Castro, C.A., Hogan, J.B., Benson, K.A., Shehata, C.W., Landauer, M.R. (1995) Behavioral effects of vehicles: DMSO,
ethanol, Tween-20, Tween-80, and Emulphor-620. Pharmacol. Biochem. Behav. 50:521–526.
Conwell, C.C., Huang, L. (2005) Recent advances in non-viral gene delivery. Adv. Genet. 53:1–18.
Centers for Disease Control and Prevention (1999) Summary of notifiable diseases. United States. 1998. Morb. Mortal
Wkly Rep. 47:11-23.
Dahmane, T., Giusti, F., Catoire, L.J., Popot, J.-L. (2011) Sulfonated amphipols: Synthesis, properties and applications.
Biopolymers 95:811–823.
de la Maza, L.M., Peterson, E.M. (2002) Vaccines for Chlamydia trachomatis infections. Curr. Opin. Invest. Drugs
3:980–986.
Diab, C., Tribet, C., Gohon, Y., Popot, J.-L., Winnik, F.M. (2007a) Complexation of integral membrane proteins by
phosphorylcholine-based amphipols. Biochim. Biophys. Acta 1768:2737–2747.
Diab, C., Winnik, F.M., Tribet, C. (2007b) Enthalpy of interaction and binding isotherms of non-ionic surfactants onto
micellar amphiphilic polymers (amphipols). Langmuir 23:3025–3035.
Dong-Ji, Z., Yang, X., Shen, C., Lu, H., Murdin, A., Brunham, R.C. (2000) Priming with Chlamydia trachomatis major
outer membrane protein (MOMP) DNA followed by MOMP ISCOM boosting enhances protection and is associated
with increased immunoglobulin A and Th1 cellular immune responses. Infect. Immun. 68:3074–3078.
Doolan, D.L., Apte, S.H., Proietti, C. (2015) Genome-based vaccine design: the promise for malaria and other infectious
diseases. Int. J. Parasitol. 44:901–913.
Duarte, A.M.S., Wolfs, C.J.A.M., Koehorsta, R.B.M., Popot, J.-L., Hemminga, M.A. (2008) Solubilization of V-ATPase
transmembrane peptides by amphipol A8-35. J. Peptide Chem. 14:389–393.
Elwell, C., Mirrashidi, K., Engel, J. (2016) Chlamydia cell biology and pathogenesis. Nat. Rev. Microbiol. 14:385–400.
Farris, C.M., Morrison, R.P. (2011) Vaccination against Chlamydia genital infection utilizing the murine C. muridarum
model. Infect. Immun. 79:986–996.
Farris, C.M., Morrison, S.G., Morrison, R.P. (2010) CD4
+ T cells and antibody are required for optimal major outer
membrane protein vaccine-induced immunity to Chlamydia muridarum genital infection. Infect. Immun.
78:4374–4383
Feher, V.A., Randall, A., Baldi, P., Bush, R.M., de la Maza, L.M., Amaro, R.R. (2013) A three-dimensional trimeric
β-barrel model for Chlamydia MOMP contains conserved and novel elements of Gram-negative bacterial porins.
PLoS One 8:e68934.
Feinstein, H.E., Tifrea, D., Sun, G., Popot, J.-L., de la Maza, L.M., Cocco, M.J. (2014) Long-term stability of a vaccine
formulated with the amphipol-trapped major outer membrane protein from Chlamydia trachomatis. J. Membr. Biol.
247:1053–1065.
Fernandez, A., Le Bon, C., Baumlin, N., Giusti, F., Crémel, G., Popot, J.-L., Bagnard, D. (2014) In vivo characterization
of the biodistribution profile of amphipols J. Membr. Biol. 247:1043–1051.
Gohon, Y. (1996) Etude des interactions entre un analogue du fragment transmembranaire de la glycophorine A et des
polymères amphiphiles: les amphipols. Rapport de DEA, Université Paris VI, Paris, 28 p.
Götz, H., Lindback, J., Ripa, T., Arneborn, M., Ramsted, K., Ekdahl, K. (2002) Is the increase in notifications of
Chlamydia trachomatis infections in Sweden the result of changes in prevalence, sampling frequency or diagnostic
methods? Scand. J. Infect. Dis. 34:28–34.
Grayston, J.T., Wang, S.P. (1978) The potential for vaccine against infection of the genital tract with Chlamydia
trachomatis. Sex. Transm. Dis. 5:73–77.
Han, S.G., Na, J.H., Lee, W.K., Park, D., Oh, J., Yoon, S.H., Lee, C.K., Sung, M.H., Shin, Y.K., Yu, Y.G. (2014) An
amphipathic polypeptide derived from poly-γ-glutamic acid for the stabilization of membrane proteins. Prot. Sci.
23:1800–1807.
Hubert, P., Sawma, P., Duneau, J.-P., Khao, J., Henin, J., Bagnard, D., Sturgis, J. (2010) Single-spanning transmembrane
domains in cell growth and cell-cell interactions: More than meets the eye? Cell Adh. Migr. 4:313–324.
References
679
envelope protein induced by liposomal adjuvant formulations containing monophosphoryl lipid A with or without
QS21. Vaccine 33:5578–5587.
Blake, M.S., Wetzler, L.M. (1995) Vaccines for gonorrhea: where are we on the curve? Trends Microbiol. 3:469–474.
Blankson, H., Stakkestad, J.A., Fagertun, H., Thom, E., Wadstein, J., Gudmundsen, O. (2000) Conjugated linoleic acid
reduces body fat mass in overweight and obese humans. J. Nutr. 130:2943–2948.
Bobbala, S., Hook, S. (2016) Is there an optimal formulation and delivery strategy for subunit vaccines? Pharm. Res.
33:2078–2097.
Brunham, R.C., Rey-Ladino, J. (2005) Immunology of Chlamydia infection: implications for a Chlamydia trachomatis
vaccine. Nature Rev. Immunol. 5:149–161.
Cai, S., He, F., Samra, H.S., de la Maza, L.M., Bottazzi, M., Joshi, S.B., Middaugh, C.R. (2009) Biophysical and
stabilization studies of the Chlamydia trachomatis mouse pneumonitis major outer membrane protein. Mol. Pharm.
6:1553–1561.
Brunham, R.C., Pourbohloul, B., Mak, S., White, R., Rekart, M.L. (2005) The unexpected impact of a Chlamydia
trachomatis infection control program on susceptibility to reinfection. J. Infect. Dis. 192:1836–1844.
Castro, C.A., Hogan, J.B., Benson, K.A., Shehata, C.W., Landauer, M.R. (1995) Behavioral effects of vehicles: DMSO,
ethanol, Tween-20, Tween-80, and Emulphor-620. Pharmacol. Biochem. Behav. 50:521–526.
Conwell, C.C., Huang, L. (2005) Recent advances in non-viral gene delivery. Adv. Genet. 53:1–18.
Centers for Disease Control and Prevention (1999) Summary of notifiable diseases. United States. 1998. Morb. Mortal
Wkly Rep. 47:11-23.
Dahmane, T., Giusti, F., Catoire, L.J., Popot, J.-L. (2011) Sulfonated amphipols: Synthesis, properties and applications.
Biopolymers 95:811–823.
de la Maza, L.M., Peterson, E.M. (2002) Vaccines for Chlamydia trachomatis infections. Curr. Opin. Invest. Drugs
3:980–986.
Diab, C., Tribet, C., Gohon, Y., Popot, J.-L., Winnik, F.M. (2007a) Complexation of integral membrane proteins by
phosphorylcholine-based amphipols. Biochim. Biophys. Acta 1768:2737–2747.
Diab, C., Winnik, F.M., Tribet, C. (2007b) Enthalpy of interaction and binding isotherms of non-ionic surfactants onto
micellar amphiphilic polymers (amphipols). Langmuir 23:3025–3035.
Dong-Ji, Z., Yang, X., Shen, C., Lu, H., Murdin, A., Brunham, R.C. (2000) Priming with Chlamydia trachomatis major
outer membrane protein (MOMP) DNA followed by MOMP ISCOM boosting enhances protection and is associated
with increased immunoglobulin A and Th1 cellular immune responses. Infect. Immun. 68:3074–3078.
Doolan, D.L., Apte, S.H., Proietti, C. (2015) Genome-based vaccine design: the promise for malaria and other infectious
diseases. Int. J. Parasitol. 44:901–913.
Duarte, A.M.S., Wolfs, C.J.A.M., Koehorsta, R.B.M., Popot, J.-L., Hemminga, M.A. (2008) Solubilization of V-ATPase
transmembrane peptides by amphipol A8-35. J. Peptide Chem. 14:389–393.
Elwell, C., Mirrashidi, K., Engel, J. (2016) Chlamydia cell biology and pathogenesis. Nat. Rev. Microbiol. 14:385–400.
Farris, C.M., Morrison, R.P. (2011) Vaccination against Chlamydia genital infection utilizing the murine C. muridarum
model. Infect. Immun. 79:986–996.
Farris, C.M., Morrison, S.G., Morrison, R.P. (2010) CD4
+ T cells and antibody are required for optimal major outer
membrane protein vaccine-induced immunity to Chlamydia muridarum genital infection. Infect. Immun.
78:4374–4383
Feher, V.A., Randall, A., Baldi, P., Bush, R.M., de la Maza, L.M., Amaro, R.R. (2013) A three-dimensional trimeric
β-barrel model for Chlamydia MOMP contains conserved and novel elements of Gram-negative bacterial porins.
PLoS One 8:e68934.
Feinstein, H.E., Tifrea, D., Sun, G., Popot, J.-L., de la Maza, L.M., Cocco, M.J. (2014) Long-term stability of a vaccine
formulated with the amphipol-trapped major outer membrane protein from Chlamydia trachomatis. J. Membr. Biol.
247:1053–1065.
Fernandez, A., Le Bon, C., Baumlin, N., Giusti, F., Crémel, G., Popot, J.-L., Bagnard, D. (2014) In vivo characterization
of the biodistribution profile of amphipols J. Membr. Biol. 247:1043–1051.
Gohon, Y. (1996) Etude des interactions entre un analogue du fragment transmembranaire de la glycophorine A et des
polymères amphiphiles: les amphipols. Rapport de DEA, Université Paris VI, Paris, 28 p.
Götz, H., Lindback, J., Ripa, T., Arneborn, M., Ramsted, K., Ekdahl, K. (2002) Is the increase in notifications of
Chlamydia trachomatis infections in Sweden the result of changes in prevalence, sampling frequency or diagnostic
methods? Scand. J. Infect. Dis. 34:28–34.
Grayston, J.T., Wang, S.P. (1978) The potential for vaccine against infection of the genital tract with Chlamydia
trachomatis. Sex. Transm. Dis. 5:73–77.
Han, S.G., Na, J.H., Lee, W.K., Park, D., Oh, J., Yoon, S.H., Lee, C.K., Sung, M.H., Shin, Y.K., Yu, Y.G. (2014) An
amphipathic polypeptide derived from poly-γ-glutamic acid for the stabilization of membrane proteins. Prot. Sci.
23:1800–1807.
Hubert, P., Sawma, P., Duneau, J.-P., Khao, J., Henin, J., Bagnard, D., Sturgis, J. (2010) Single-spanning transmembrane
domains in cell growth and cell-cell interactions: More than meets the eye? Cell Adh. Migr. 4:313–324.
References
679