Bioprospecting by Phage Display of Mimetic Peptides of Chlamydia trachomatis for Use in Laboratory Diagnosis

References

• Schachter J, Caldwell HD. Chlamydiae. Annu Rev Microbiol. 1980;34:285–309. doi:10.1146/annurev.mi.34.100180.001441
   PubMed Web of Science ®Google Scholar
• Weinstock H, Dean D, Bolan G. Chlamydia trachomatis infection. Infect Dis Clin North Am. 1994;8:797–819.
   PubMed Web of Science ®Google Scholar
• Inman RD, Whittum-Hudson JA, Schumacher HR, Hudson AP. Chlamydia and associated arthritis. Curr Opin Rheumatol. 2000;12:254–262. doi:10.1097/00002281-200007000-00004
   PubMed Web of Science ®Google Scholar
• Witkin SS, Minis E, Athanasiou A, Leizer J, Linhares IM. Chlamydia trachomatis: the Persistent Pathogen. Clin Vaccine Immunol. 2017;24(10):e00203–17. doi:10.1128/CVI.00203-17
   PubMedGoogle Scholar
• den Heijer CDJ, Hoebe CJPA, Driessen JHM, et al. Chlamydia trachomatis and the Risk of Pelvic Inflammatory Disease, Ectopic Pregnancy, and Female Infertility: a Retrospective Cohort Study Among Primary Care Patients. Clin Infect Dis. 2019;69(9):1517–1525. doi:10.1093/cid/ciz429
   PubMed Web of Science ®Google Scholar
• World Health Organization. Sexually transmitted infections; 2019. Available from: https://www.who.int/news-room/fact-sheets/detail/sexually-transmitted-infections-(stis). Accessed December 12, 2021.
   Google Scholar
• Matsumoto A. Electron microscopic observations of surface projections on Chlamydia psittaci reticulate bodies. J Bacteriol. 1982;150(1):358–364. doi:10.1128/jb.150.1.358-364.1982
   Web of Science ®Google Scholar
• Abdelrahman YM, Belland RJ. The chlamydial developmental cycle. FEMS Microbiol Rev. 2005;29:949–959. doi:10.1016/j.femsre.2005.03.002
   PubMed Web of Science ®Google Scholar
• Moulder JW. The relation of the psittacosis group (Chlamydiae) to bacteria and viruses. Annu Rev Microbiol. 1966;20:107–130. doi:10.1146/annurev.mi.20.100166.000543
   Web of Science ®Google Scholar
• Elwell C, Mirrashidi K, Engel J. Chlamydia cell biology and pathogenesis. Nat Rev Microbiol. 2016;14(6):385–400. doi:10.1038/nrmicro.2016.30
   PubMed Web of Science ®Google Scholar
• Solomon AW, Peeling RW, Foster A, Mabey DCW. Diagnosis and Assessment of Trachoma. Clin Microbiol Rev. 2004;17(4):982–1011. doi:10.1128/CMR.17.4.982-1011.2004
   PubMed Web of Science ®Google Scholar
• Caldwell HD, Kromhout J, Schachter J. Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis. Infect Immun. 1981;31(3):1161–1176. doi:10.1128/iai.31.3.1161-1176.1981
   PubMed Web of Science ®Google Scholar
• Hatch TP, Miceli M, Sublett JE. Synthesis of disulfide-bonded outer membrane proteins during the developmental cycle of Chlamydia psittaci and Chlamydia trachomatis. J Bacteriol. 1986;165(2):379–385. doi:10.1128/jb.165.2.379-385.1986
   Web of Science ®Google Scholar
• Stephens RS, Sanchez-Pescador R, Wagar EA. Diversity of Chlamydia trachomatis major outer membrane protein genes. J Bacteriol. 1987;169(9):3879–3885. doi:10.1128/jb.169.9.3879-3885.1987
   Web of Science ®Google Scholar
• Morré SA, Ossewaarde JM, Lan J, et al. Serotyping and Genotyping of Genital Chlamydia trachomatis Isolates Reveal Variants of Serovars Ba, G, and J as Confirmed by omp1 Nucleotide Sequence Analysis. J Clin Microbiol. 1998;36(2):345–351. doi:10.1128/JCM.36.2.345-351
   Web of Science ®Google Scholar
• Kari L, Whitmire WM, Crane DD, et al. Chlamydia trachomatis native major outer membrane protein induces partial protection in nonhuman primates: implication for a trachoma transmission-blocking vaccine. J Immunol. 2009;182(12):8063–8070. doi:10.4049/jimmunol.0804375
   Web of Science ®Google Scholar
• Kariagina AS, Alekseevskiĭ AV, Spirin SA, Zigangirova NA, Gintsburg AL. Effector proteins of Chlamydia. Mol Biol (Mosk). 2009;43(6):963–983.
   Web of Science ®Google Scholar
• Treharne JD, Forsey T, Thomas BJ. Chlamydial serology. Br Med Bull. 1983;39(2):194–200. doi:10.1093/oxfordjournals.bmb.a071815
   Web of Science ®Google Scholar
• Ozanne G, Lefebvre J. Specificity of the microimmunofluorescence assay for the serodiagnosis of Chlamydia pneumoniae infections. Can J Microbiol. 1992;38(11):1185–1189. doi:10.1139/m92-194
   Web of Science ®Google Scholar
• Herkenhoff ME, Gaulke R, Vieira LL, Ferreira OS, Pitlovanciv AK, Remualdo VR. Prevalência de Chlamydia trachomathis em amostras endocervicais de mulheres em São Paulo e Santa Catarina pela PCR. J Bras Patol Med Lab. 2012;48(5):323–327. doi:10.1590/S1676-24442012000500004
   Google Scholar
• Brasil. Ministério da Saúde. Diagnóstico Laboratorial da Clamídia; 1997. Available from: https://bvsms.saude.gov.br/bvs/publicacoes/cd05_09.pdf. Accessed May 17, 2022.
   Google Scholar
• Black CM. Current methods of laboratory diagnosis of Chlamydia trachomatis infections. Clin Microbiol Rev. 1997;10(1):160–184. doi:10.1128/CMR.10.1.160
   PubMed Web of Science ®Google Scholar
• Hamdad F, Orfila J, Boulanger JC, Eb F. Chlamydia trachomatis urogenital infections in women. Best diagnostic approaches. Gynecol Obstet Fertil. 2004;32(12):1064–1074. doi:10.1016/j.gyobfe.2004.10.017
   Google Scholar
• Jackson B. Relative cost-effectiveness of different tests for Chlamydia trachomatis. Ann Intern Med. 2005;142(4):308. doi:10.7326/0003-4819-142-4-200502150-00019
   Web of Science ®Google Scholar
• Persson K. The role of serology, antibiotic susceptibility testing and serovar determination in genital chlamydial infections. Best Pract Res Clin Obstet Gynaecol. 2002;16(6):801–814. doi:10.1053/beog.2002.0321
   Web of Science ®Google Scholar
• Johnson AM, Horner P. A new role for Chlamydia trachomatis serology? Sex Transm Infect. 2008;84(2):79–80. doi:10.1136/sti.2007.028472
   Web of Science ®Google Scholar
• Ishak M, Costa MM, Almeida NC, et al. Chlamydia trachomatis serotype A infections in the Amazon region of Brazil: prevalence, entry and dissemination. Rev Soc Bras Med Trop. 2015;48(2):170–174. doi:10.1590/0037-8682-0038-2015
   Web of Science ®Google Scholar
• Ferreira GRON, Freitas FB, Queiroz MAF, et al. Epidemiology and risk factors for Chlamydia trachomatis, Treponema pallidum, Hepatitis B Virus and Hepatitis C Virus in the Marajó Archipelago, Brazilian Amazon. J Community Med Health Educ. 2019;9:643. doi:10.4172/2161-0711.1000643
   Google Scholar
• Rahman KS, Kaltenboeck B. Multipeptide assays for sensitive and differential detection of anti-chlamydia trachomatis antibodies. J Infect Dis. 2021;224(12 Suppl 2):S86–S95. doi:10.1093/infdis/jiab016
   Web of Science ®Google Scholar
• Rahman KS, Darville T, Russell AN, et al. Discovery of Human-Specific Immunodominant Chlamydia trachomatis B Cell Epitopes. mSphere. 2018;3(4):e00246–18. doi:10.1128/mSphere.00246-18
   Web of Science ®Google Scholar
• Smith GP, Petrenko VA. Phage Display. Chem Rev. 1997;97(2):391–410. doi:10.1021/cr960065d
   PubMed Web of Science ®Google Scholar
• Arap MA. Phage display technology – applications and innovations. Genet Mol Biol. 2005;28(1):1–9. doi:10.1590/S1415-47572005000100001
   Web of Science ®Google Scholar
• Silva JRA, Kawazoe U. Avian anticoccidial activity of a novel membrane interactive peptide selected from phage display libraries. Mol Biochem Parasitol. 2002;120(1):53–60. doi:10.1016/s0166-6851(01
   Web of Science ®Google Scholar
• Pande J, Szewczyk MM, Grover AK. Phage display: concept, innovations, applications and future. Biotechnol Adv. 2010;28(6):849–858. doi:10.1016/j.biotechadv.2010.07.004
   PubMed Web of Science ®Google Scholar
• Lopes RS, Queiroz MAF, Gomes STM, Vallinoto ACR, Goulart LR, Ishak R. Phage display: an important tool in the discovery of peptides with anti-HIV activity. Biotechnol Adv. 2018;36(7):1847–1854. doi:10.1016/j.biotechadv.2018.07.003
   Web of Science ®Google Scholar
• Martins IM, Reis RL, Azevedo HS. Phage Display Technology in Biomaterials Engineering: progress and Opportunities for Applications in Regenerative Medicine. ACS Chem Biol. 2016;11:2962–2980. doi:10.1021/acschembio.5b00717
   PubMed Web of Science ®Google Scholar
• Saw PE, Song EW. Phage display screening of therapeutic peptide for cancer targeting and therapy. Protein Cell. 2019;10(11):787–807. doi:10.1007/s13238-019-0639-7
   PubMed Web of Science ®Google Scholar
• Portes LDS, Kioshima ES, de Camargo ZP, Batista WL, Xander P. Subtractive phage display selection for screening and identification of peptide sequences with potential use in serodiagnosis of paracoccidioidomycosis caused by Paracoccidioides brasiliensis. Lett Appl Microbiol. 2017;65(5):346–353. doi:10.1111/lam.12788
   Web of Science ®Google Scholar
• Moreira GMSG, Köllner SMS, Helmsing S, et al. Pyruvate dehydrogenase complex-enzyme 2, a new target for Listeria spp. detection identified using combined phage display technologies. Sci Rep. 2020;10(1):15267. doi:10.1038/s41598-020-72159-4
   Web of Science ®Google Scholar
• Barbas CF, Burto DR, Scott JK, Silverino GJ. Phage Display: A Laboratory Manual. New York: Cold Spring Harbor Laboratory Press; 2001.
   Google Scholar
• Scheurwater E, Reid CW, Clarke AJ. Lytic transglycosylases: bacterial space-making autolysins. Int J Biochem Cell Biol. 2008;40(4):586–591. doi:10.1016/j.biocel.2007.03.018
   Web of Science ®Google Scholar
• Vermassen A, Leroy S, Talon R, Provot C, Popowska M, Desvaux M. Cell Wall Hydrolases in Bacteria: insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan. Front Microbiol. 2019;10:331. doi:10.3389/fmicb.2019.00331
   PubMed Web of Science ®Google Scholar
• Paoletti L, Lu YJ, Schujman GE, de Mendoza D, Rock CO. Coupling of fatty acid and phospholipid synthesis in Bacillus subtilis. J Bacteriol. 2007;189(16):5816–5824. doi:10.1128/JB.00602-07
   Web of Science ®Google Scholar
• Lu YJ, Zhang F, Grimes KD, Lee RE, Rock CO. Topology and active site of PlsY: the bacterial acylphosphate: glycerol-3-phosphateacyltransferase. J Biol Chem. 2007;282(15):11339–11346. doi:10.1074/jbc.M700374200
   Web of Science ®Google Scholar
• Yang M, Rajeeve K, Rudel T, Dandekar T. Comprehensive Flux Modeling of Chlamydia trachomatis Proteome and qRT-PCR Data Indicate Biphasic Metabolic Differences Between Elementary Bodies and Reticulate Bodies During Infection. Front Microbiol. 2019;10:2350. doi:10.3389/fmicb.2019.02350
   Web of Science ®Google Scholar
• Fan C, Wu YH, Decker CM, et al. Defensive Function of Transposable Elements in Bacteria. ACS Synth Biol. 2019;8(9):2141–2151. doi:10.1021/acssynbio.9b00218
   Web of Science ®Google Scholar
• O’Neill CE, Skilton RJ, Forster J, et al. An inducible transposon mutagenesis approach for the intracellular human pathogen Chlamydia trachomatis. Wellcome Open Res. 2021;6:312. doi:10.12688/wellcomeopenres
   Google Scholar
• Du K, Fuyan Wang F, Wang ZHJ, Cheng W, Li M, Yu P. Localization and Characterization of GTP-Binding Protein CT703 in the Chlamydia trachomatis-Infected Cells. Curr Microbiol. 2011;62(2):465–471. doi:10.1007/s00284-010-9730-2
   Web of Science ®Google Scholar
• Huang Z, Feng Y, Chen D, et al. Structural basis for activation and inhibition of the secreted chlamydia protease CPAF. Cell Host Microbe. 2008;4(6):529–542. doi:10.1016/j.chom.2008.10.005
   Web of Science ®Google Scholar
• Chen AL, Johnson KA, Lee JK, Sütterlin C, Tan M. CPAF: a Chlamydial protease in search of an authentic substrate. PLoS Pathog. 2012;8(8):e1002842. doi:10.1371/journal.ppat.1002842
   Web of Science ®Google Scholar
• Dong F, Sharma J, Xiao Y, Zhong Y, Zhong G. Intramolecular dimerization is required for the chlamydia-secreted protease CPAF to degrade host transcriptional factors. Infect Immun. 2004;72(7):3869–3875. doi:10.1128/IAI.72.7.3869-3875.2004
   Web of Science ®Google Scholar
• Paschen SA, Christian JG, Vier J, et al. Cytopathicity of Chlamydia is largely reproduced by expression of a single chlamydial protease. J Cell Biol. 2008;182(1):117–127. doi:10.1083/jcb.200804023
   Web of Science ®Google Scholar
• Snavely EA, Kokes M, Dunn JD, et al. Reassessing the role of the secreted protease CPAF in Chlamydia trachomatis infection through genetic approaches. Pathog Dis. 2014;71(3):336–351. doi:10.1111/2049-632X.12179
   Web of Science ®Google Scholar
• Patton MJ, McCorrister S, Grant C, et al. Chlamydial Protease-Like Activity Factor and Type III Secreted Effectors Cooperate in Inhibition of p65 Nuclear Translocation. mBio. 2016;7(5):e01427–16. doi:10.1128/mBio.01427-16
   Web of Science ®Google Scholar
• Dong F, Zhong Y, Arulanandam B, Zhong G. Production of a proteolytically active protein, chlamydial protease/proteasome-like activity factor, by five different Chlamydia species. Infect Immun. 2005;73(3):1868–1872. doi:10.1128/IAI.73.3.1868-1872.2005
   Web of Science ®Google Scholar
• Larralde O, Petrik J. Phage-displayed peptides that mimic epitopes of hepatitis E virus capsid. Med Microbiol Immunol. 2017;206(4):301–309. doi:10.1007/s00430-017-0507-0
   Web of Science ®Google Scholar
• Wang L, Deng X, Liu H, et al. The mimic epitopes of Mycobacterium tuberculosis screened by phage display peptide library have serodiagnostic potential for tuberculosis. Pathog Dis. 2016;74(8):ftw091. doi:10.1093/femspd/ftw091
   PubMed Web of Science ®Google Scholar
• Feliciano ND, Ribeiro VS, Gonzaga HT, et al. Short epitope-based synthetic peptides for serodiagnosis of human strongyloidiasis. Immunol Lett. 2016;172:89–93. doi:10.1016/j.imlet.2016.03.002
   Web of Science ®Google Scholar
• Lindquist EA, Marks JD, Kleba BJ, Sthens RS. Phage-display antibody detection of Chlamydia trachomatis-associated antigens. Microbiology. 2002;148(Pt 2):443–451. doi:10.1099/00221287-148-2-443
   Web of Science ®Google Scholar
• Franco GM, Rocha AS, Cox LJ, et al. Multi-Epitope Protein as a Tool of Serological Diagnostic Development for HTLV-1 and HTLV-2 Infections. Front Public Health. 2022;10:884701. doi:10.3389/fpubh.2022.884701
   Web of Science ®Google Scholar
• Li W, Murthy AK, Guentzel MN, et al. Antigen-specific CD4+ T cells produce sufficient IFN-gamma to mediate robust protective immunity against genital Chlamydia muridarum infection. J Immunol. 2008;180(5):3375–3382. doi:10.4049/jimmunol.180.5.3375
   PubMed Web of Science ®Google Scholar