DAFTAR PUSTAKA

1. Alena Klochko, M. Salmonella Infection (Salmonellosis). 2017 [cited 2018 January

6]; Available from: https://emedicine.medscape.com/article/228174-overview.
2. Nester, E.W., D.A. Jr, and C.E. Roberts, Microbiology: a Human Perspective. 7th ed.
2012: Mc-Graw Hill, New York, NY, USA.
3. Setiabudy, R. and Y. Mariana, Sulfonamid, Kotrimoksazol, dan Antiseptik

Saluran Kemih, in Farmakologi dan Terapi. 2007, Departemen Farmakologi dan

Terapeutik Fakultas

Kedokteran Universitas Indonesia: Jakarta, Indonesia. p. 584–596.

4. Guo, C., et al., Curcumin induces human cathelicidin antimicrobial peptide gene
expression through a vitamin D receptor-independent pathway. J Nutr Biochem,
2013. 24(5): p. 754-9.
5. Tajbakhsh, S., et al., Antibacterial activity of indium curcumin and indium
diacetylcurcumin. Vol. 7. 2008. 3832-3835.
6. Robertson , R.P.L., et al., Evaluation of Chloramphenicol and Ampicillin in
Salmonella Enteric Fever. New England Journal of Medicine, 1968. 278(4): p. 171-
176.
7. Butler, T., L. Rumans, and K. Arnold, Response of typhoid fever caused by
chloramphenicol-susceptible and chloramphenicol-resistant strains of Salmonella
typhi to treatment with trimethoprim-sulfamethoxazole. Rev Infect Dis, 1982. 4(2):
p. 551-61.
8. Lampe, R.M., C. Duangmani, and P. Mansuwan, Chloramphenicol- and ampicillin-
resistant typhoid fever. JAMA, 1975. 233(7): p. 768-768.
9. Crump, J.A. and E.D. Mintz, Global trends in typhoid and paratyphoid fever. Clinical
infectious diseases : an official publication of the Infectious Diseases Society of
America, 2010. 50(2): p. 241-246.
10. Kariuki, S., et al., Typhoid in Kenya is associated with a dominant multidrug-
resistant Salmonella enterica serovar Typhi haplotype that is also widespread in
Southeast Asia. J Clin Microbiol, 2010. 48(6): p. 2171-6.
11. Dolecek, C., et al., A multi-center randomised controlled trial of gatifloxacin versus
azithromycin for the treatment of uncomplicated typhoid fever in children and
adults in Vietnam. PLoS One, 2008. 3(5): p. e2188.
12. Kumar, Y., A. Sharma, and K. Mani, High Level of Resistance to nalidixic acid in
Salmonella enterica serovar Typhi in Central India. Vol. 3. 2009. 467-9.
13. Dong, B.-Q., et al., Trends and disease burden of enteric fever in Guangxi province,
China, 1994–2004. Bulletin of the World Health Organization, 2010. 88(9): p. 689-
696.
14. Nizet, V. and R.L. Gallo, Cathelicidins and innate defense against invasive bacterial
infection. Scand J Infect Dis, 2003. 35(9): p. 670-6.
15. Achmad, S.A., et al., Ilmu kimia dan kegunaan tumbuh-tumbuhan obat Indonesia.
Intitute Teknologi Bandung, Indonesia, 2007.
16. Chattopadhyay, I., et al., Turmeric and curcumin: Biological actions and medicinal
applications. Current Science, 2004. 87(1): p. 44-53.
17. Brat, P., F. Tourniaire, and M.-J. Amiot-Carlin, Stability and Analysis of Phenolic
Pigments. 2007. 71-86.
18. Rustam, E., L. Atmasari, and Yanwirasti, Efek Antiinflamasi Ekstrak Etanol Kunyit
(Curcuma domestica Val) Pada Tikus Jantan Galur Wistar. Jurnal Sains dan
Teknologi Farmasi, 2007. 12: p. 112-115.
19. Jurenka, J.S., Anti-inflammatory properties of curcumin, a major constituent of
Curcuma longa: a review of preclinical and clinical research. Altern Med Rev, 2009.
14(2): p. 141-53.
20. Chainani-Wu, N., Safety and anti-inflammatory activity of curcumin: a component
of tumeric (Curcuma longa). J Altern Complement Med, 2003. 9(1): p. 161-8.
21. Minghetti, L., Cyclooxygenase-2 (COX-2) in inflammatory and degenerative brain
diseases. J Neuropathol Exp Neurol, 2004. 63(9): p. 901-10.
22. Ravindran, J., et al., Bisdemethylcurcumin and structurally related hispolon
analogues of curcumin exhibit enhanced prooxidant, anti-proliferative and anti-
inflammatory activities in vitro. Biochem Pharmacol, 2010. 79(11): p. 1658-66.
23. Jacob, A., et al., Mechanism of the Anti-inflammatory Effect of Curcumin: PPAR-
gamma Activation. PPAR Res, 2007. 2007: p. 89369.
24. Aznam, N., Uji Aktivitas Ekstrak Kunyit (Curcuma domestica, Val). Prosiding
Seminar nasional, Penelitian, Pendidikan dan Penerapan MIPA. FMIPA UNY
Yogyakarta, 2004.
25. Majeed, M., V. Badmaev, and S. R n D Team, Curcuminoids - antioxidant
phytonutrients. 2003.
26. Venkatesan, P., et al., Effect of curcumin analogues on oxidation of haemoglobin
and lysis of erythrocytes. Vol. 84. 2003. 74-78.
27. Huang, M.T., et al., Inhibitory effects of curcumin on tumor initiation by
benzo[a]pyrene and 7,12-dimethylbenz[a]anthracene. Carcinogenesis, 1992.
13(11): p. 2183-6.
28. Ramprasad, C. and M. Sirsi, Studies on Indian medicinal plants: Curcuma longa
Linn. - Effect of curcumin and the essential oils of Curcuma longa on bile secretion.
Vol. 15. 1956. 262-265.
29. SHIH, A.L. and N.D. HARRIS, Antimicrobial Activity of Selected Antioxidants.
Journal of Food Protection, 1977. 40(8): p. 520-522.
30. Sihombing, P.A., Aplikasi Ekstrak Kunyit (Curcuma domestica) sebagai bahan
pengawet mie basah. Fakultas Teknologi Pertanian Departemen Ilmu Dan
Teknologi Pangan Institut Pertanian Bogor, 2007.
31. Winarsih, S., H. Mudjiwijono, and D.T. Sari, EFEK ANTIBAKTERI EKSTRAK ETANOL
RIMPANG KUNYIT (Curcuma domestica) TERHADAP PERTUMBUHAN Shigella
dysenteriae ISOLAT 2312-F SECARA IN VITRO.
32. Fauzah, S.N. and I.A. Zulfah, Pengaruh Pemberian Berbagai Konsentrasi Ekstrak
Kunyit (Curcuma Longa) terhadap pertumbuhan Escherchia Coli Fakultas
Kedokteran Universitas Swadaya Gunung Jati Cirebon
33. Warnaini, C., UJI EFEKTIVITAS EKSTRAK KUNYIT SEBAGAI ANTIBAKTERI TERHADAP
PERTUMBUHAN BAKTERI Bacillus sp. dan Shigella dysentriae SECARA IN VITRO.
34. Yuliati, Uji Efektivitas Ekstrak Kunyit Sebagai Anti Bakteri dalam pertumbuhan
Bacillus sp dan Shigela dysentriae secara in vitro. Jurnal Profesi Medika 2016. 10.
35. Tyagi, P., et al., Bactericidal Activity of Curcumin I Is Associated with Damaging of
Bacterial Membrane. PLoS ONE, 2015. 10(3): p. e0121313.
36. Rai, D., et al., Curcumin inhibits FtsZ assembly: an attractive mechanism for its
antibacterial activity. Biochem J, 2008. 410(1): p. 147-55.
37. Wang, J., et al., Curcumin protects mice from Staphylococcus aureus pneumonia by
interfering with the self-assembly process of alpha-hemolysin. Sci Rep, 2016. 6: p.
28254.
38. Siwipeni Irmawanti Rahayu, Nurdiana Nurdiana, and S. Santoso, The Effect of
Curcumin and Cotrimoxazole in Salmonella Typhimurium Infection In Vivo. ISRN
Microbiology, 2013. 2013: p. 4.
39. Brogden, K.A., Antimicrobial peptides: pore formers or metabolic inhibitors in
bacteria? Nat Rev Microbiol, 2005. 3(3): p. 238-50.
40. Giuliani, A., G. Pirri, and S.F. Nicoletto, Antimicrobial peptides: an overview of a
promising class of therapeutics. Central European Journal of Biology, 2007. 2(1): p.
1-33.
41. Steinmann, J., Induction and regulation of CAMP gene expression, in Department
of Biology2008, University of Iceland: Reykjavík, Iceland.
42. Ganz, T., Defensins: antimicrobial peptides of innate immunity. Nat Rev Immunol,
2003. 3(9): p. 710-20.
43. Pazgier, M., et al., Human beta-defensins. Cell Mol Life Sci, 2006. 63(11): p. 1294-
313.
44. Durr, U.H., U.S. Sudheendra, and A. Ramamoorthy, LL-37, the only human member
of the cathelicidin family of antimicrobial peptides. Biochim Biophys Acta, 2006.
1758(9): p. 1408-25.
45. Zanetti, M., Cathelicidins, multifunctional peptides of the innate immunity. J
Leukoc Biol, 2004. 75(1): p. 39-48.
46. Zaiou, M., V. Nizet, and R.L. Gallo, Antimicrobial and protease inhibitory functions
of the human cathelicidin (hCAP18/LL-37) prosequence. J Invest Dermatol, 2003.
120(5): p. 810-6.
47. Zanetti, M., R. Gennaro, and D. Romeo, Cathelicidins: a novel protein family with a
common proregion and a variable C-terminal antimicrobial domain. FEBS Lett,
1995. 374(1): p. 1-5.
48. Ramanathan, B., et al., Cathelicidins: microbicidal activity, mechanisms of action,
and roles in innate immunity. Microbes Infect, 2002. 4(3): p. 361-72.
49. Pestonjamasp, V.K., K.H. Huttner, and R.L. Gallo, Processing site and gene
structure for the murine antimicrobial peptide CRAMP. Peptides, 2001. 22(10): p.
1643-50.
50. Gudmundsson, G.H., et al., The human gene FALL39 and processing of the cathelin
precursor to the antibacterial peptide LL-37 in granulocytes. Eur J Biochem, 1996.
238(2): p. 325-32.
51. Larrick, J.W., et al., Human CAP18: a novel antimicrobial lipopolysaccharide-
binding protein. Infection and Immunity, 1995. 63(4): p. 1291-1297.
52. Tomasinsig, L. and M. Zanetti, The cathelicidins--structure, function and evolution.
Curr Protein Pept Sci, 2005. 6(1): p. 23-34.
53. Gennaro, R. and M. Zanetti, Structural features and biological activities of the
cathelicidin-derived antimicrobial peptides. Biopolymers, 2000. 55(1): p. 31-49.
54. Johansson, J., et al., Conformation-dependent antibacterial activity of the naturally
occurring human peptide LL-37. J Biol Chem, 1998. 273(6): p. 3718-24.
55. Oren, Z., et al., Structure and organization of the human antimicrobial peptide LL-
37 in phospholipid membranes: relevance to the molecular basis for its non-cell-
selective activity. Biochemical Journal, 1999. 341(Pt 3): p. 501-513.
56. Porcelli, F., et al., NMR structure of the cathelicidin-derived human antimicrobial
peptide LL-37 in dodecylphosphocholine micelles. Biochemistry, 2008. 47(20): p.
5565-72.
57. Scott, M.G., et al., The human antimicrobial peptide LL-37 is a multifunctional
modulator of innate immune responses

J Immunol, 2002. 169(7): p. 3883-91.

58. Jeng, L., et al., Alterations in vitamin D status and anti-microbial peptide levels in
patients in the intensive care unit with sepsis. J Transl Med, 2009. 7: p. 28.
59. Sorensen, O.E., et al., Human cathelicidin, hCAP-18, is processed to the
antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood,
2001. 97(12): p. 3951-9.
60. Gombart, A.F., N. Borregaard, and H.P. Koeffler, Human cathelicidin antimicrobial
peptide (CAMP) gene is a direct target of the vitamin D receptor and is strongly up-
regulated in myeloid cells by 1,25-dihydroxyvitamin D3. FASEB J, 2005. 19(9): p.
1067-77.
61. Hase, K., et al., Expression of LL-37 by human gastric epithelial cells as a potential
host defense mechanism against Helicobacter pylori. Gastroenterology, 2003.
125(6): p. 1613-25.
62. Wu, H., et al., Regulation of cathelicidin gene expression: induction by
lipopolysaccharide, interleukin-6, retinoic acid, and Salmonella enterica serovar
typhimurium infection. Infect Immun, 2000. 68(10): p. 5552-8.
63. Islam, D., et al., Downregulation of bactericidal peptides in enteric infections: a
novel immune escape mechanism with bacterial DNA as a potential regulator. Nat
Med, 2001. 7(2): p. 180-5.
64. Bergman, P., et al., Neisseria gonorrhoeae downregulates expression of the human
antimicrobial peptide LL-37. Cell Microbiol, 2005. 7(7): p. 1009-17.
65. Wang, T.T., et al., Cutting edge: 1,25-dihydroxyvitamin D3 is a direct inducer of
antimicrobial peptide gene expression. J Immunol, 2004. 173(5): p. 2909-12.
66. Hase, K., et al., Cell differentiation is a key determinant of cathelicidin LL-
37/human cationic antimicrobial protein 18 expression by human colon
epithelium. Infect Immun, 2002. 70(2): p. 953-63.
67. Schauber, J., et al., Histone acetylation in keratinocytes enables control of the
expression of cathelicidin and CD14 by 1,25-dihydroxyvitamin D3. J Invest
Dermatol, 2008. 128(4): p. 816-24.
68. Schauber, J., et al., Expression of the cathelicidin LL-37 is modulated by short chain
fatty acids in colonocytes: relevance of signalling pathways. Gut, 2003. 52(5): p.
735-41.
69. Termen, S., et al., PU.1 and bacterial metabolites regulate the human gene CAMP
encoding antimicrobial peptide LL-37 in colon epithelial cells. Mol Immunol, 2008.
45(15): p. 3947-55.
70. Atlas, T.H.P. CAMP. [cited 2018 January 24]; Available from:
http://www.proteinatlas.org/ENSG00000164047-CAMP/tissue.
71. Travis, S.M., et al., Bactericidal activity of mammalian cathelicidin-derived
peptides. Infect Immun, 2000. 68(5): p. 2748-55.
72. De, Y., et al., Ll-37, the Neutrophil Granule–And Epithelial Cell–Derived
Cathelicidin, Utilizes Formyl Peptide Receptor–Like 1 (Fprl1) as a Receptor to
Chemoattract Human Peripheral Blood Neutrophils, Monocytes, and T Cells. The
Journal of Experimental Medicine, 2000. 192(7): p. 1069-1074.
73. Niyonsaba, F., et al., A cathelicidin family of human antibacterial peptide LL-37
induces mast cell chemotaxis. Immunology, 2002. 106(1): p. 20-6.
74. Koczulla, R., et al., An angiogenic role for the human peptide antibiotic LL-
37/hCAP-18. J Clin Invest, 2003. 111(11): p. 1665-72.
75. Heilborn, J.D., et al., The cathelicidin anti-microbial peptide LL-37 is involved in re-
epithelialization of human skin wounds and is lacking in chronic ulcer epithelium. J
Invest Dermatol, 2003. 120(3): p. 379-89.
76. Davidson, D.J., et al., The cationic antimicrobial peptide LL-37 modulates dendritic
cell differentiation and dendritic cell-induced T cell polarization. J Immunol, 2004.
172(2): p. 1146-56.
77. Burton, M.F. and P.G. Steel, The chemistry and biology of LL-37. Nat Prod Rep,
2009. 26(12): p. 1572-84.
78. Schmidtchen, A., et al., Proteinases of common pathogenic bacteria degrade and
inactivate the antibacterial peptide LL-37. Mol Microbiol, 2002. 46(1): p. 157-68.
79. Deretic, V., et al., Immunologic manifestations of autophagy. J Clin Invest, 2015.
125(1): p. 75-84.
80. Yuk, J.M., et al., Vitamin D3 induces autophagy in human
monocytes/macrophages via cathelicidin. Cell Host Microbe, 2009. 6(3): p. 231-43.
81. Songane, M., et al., The role of autophagy in host defence against Mycobacterium
tuberculosis infection. Tuberculosis (Edinb), 2012. 92(5): p. 388-96.
82. Duplantier, A.J. and M.L. van Hoek, The Human Cathelicidin Antimicrobial Peptide
LL-37 as a Potential Treatment for Polymicrobial Infected Wounds. Front Immunol,
2013. 4: p. 143.
83. Golec, M., Cathelicidin LL-37: LPS-neutralizing, pleiotropic peptide. Ann Agric
Environ Med, 2007. 14(1): p. 1-4.
84. Zaiou, M. and R.L. Gallo, Cathelicidins, essential gene-encoded mammalian
antibiotics. J Mol Med (Berl), 2002. 80(9): p. 549-61.
85. Gombart, A.F., et al., Low plasma level of cathelicidin antimicrobial peptide
(hCAP18) predicts increased infectious disease mortality in patients undergoing
hemodialysis. Clin Infect Dis, 2009. 48(4): p. 418-24.
86. Leow, L., et al., Vitamin D, innate immunity and outcomes in community acquired
pneumonia. Respirology, 2011. 16(4): p. 611-6.
87. Urrutia-Pereira, M. and D. Sole, [Vitamin D deficiency in pregnancy and its impact
on the fetus, the newborn and in childhood]. Rev Paul Pediatr, 2015. 33(1): p. 104-
13.
88. Uitterlinden, A.G., et al., Genetics and biology of vitamin D receptor
polymorphisms. Gene, 2004. 338(2): p. 143-56.
89. Sidhu, P.S., et al., Development of novel Vitamin D Receptor-Coactivator Inhibitors.
ACS Med Chem Lett, 2014. 5(2): p. 199-204.
90. Shin, J.S., et al., Vitamin D Effects on Pregnancy and the Placenta. Placenta, 2010.
31(12): p. 1027-1034.
91. Liu, P.T., et al., Toll-like receptor triggering of a vitamin D-mediated human
antimicrobial response. Science, 2006. 311(5768): p. 1770-3.
92. Vandamme, D., et al., A comprehensive summary of LL-37, the factotum human
cathelicidin peptide. Cell Immunol, 2012. 280(1): p. 22-35.
93. Prietl, B., et al., Vitamin D and immune function. Nutrients, 2013. 5(7): p. 2502-21.
94. Pinheiro da Silva, F. and M.C. Machado, Antimicrobial peptides: clinical relevance
and therapeutic implications. Peptides, 2012. 36(2): p. 308-14.
95. Bartik, L., et al., Curcumin: A Novel Nutritionally-Derived Ligand of the Vitamin D
Receptor with Implications for Colon Cancer Chemoprevention. The Journal of
nutritional biochemistry, 2010. 21(12): p. 1153-1161.
96. Dixon, B.M., et al., Positive correlation between circulating cathelicidin
antimicrobial peptide (hCAP18/LL-37) and 25-hydroxyvitamin D levels in healthy
adults. BMC Research Notes, 2012. 5: p. 575-575.
97. Brooks, G.F., et al., Jawetz, Melnick, & Adelberg's Medical Microbiology. Vol. 25th
edition. 2010: McGraw-Hill Companies, Inc.
98. Widoyono, Penyakit Tropis : Epidemiologi, Penularan, Pencegahan, dan

Pemberantasannya. 2011, Jakarta, Indonesia: Erlangga.

99. MacKenzie, K., et al., Examining the Link between Biofilm Formation and the
Ability of Pathogenic Salmonella Strains to Colonize Multiple Host Species. Vol. 4.
2017. 1-19.
100. Tumbelaka, Tata Laksana Demam Tifoid Pada Anak. Pediatrics Update. Naskah
lengkap Pendidikan Kedokteran Berkelanjutan. Ilmu Kesehatan Anak IDAI Jaya,
2003.
101. (WHO), W.H.O. Typhoid. 2015 13 April 2015 [cited 2017 January 14]; Available
from: http://www.who.int/immunization/diseases/typhoid/en/.
102. Mimi Marleni, et al., Ketepatan Uji Tubex TF® dalam Mendiagnosis Demam Tifoid
Anak

pada Demam Hari ke-4. JURNAL KEDOKTERAN DAN KESEHATAN, 2012. 1: p. 7-11.
103. Tam, F.C.H., et al., New rapid test for paratyphoid a fever: usefulness, cross-
detection, and solution. Diagnostic Microbiology and Infectious Disease, 2008.
62(2): p. 142-150.
104. J Olsen, S., et al., Evaluation of Rapid Diagnostic Test for Typhoid Fever. Vol. 42.
2004. 1885-9.
105. Ruiz, N., D. Kahne, and T.J. Silhavy, Advances in understanding bacterial outer-
membrane biogenesis. Nature Reviews Microbiology, 2006. 4: p. 57.
106. Johson, A.G., R.J. Ziegker, and L. Hawley, Essential Mikrobiologi dan Imunologi.
2011, Tanggerang, Indonesia: Bina Rupa Aksara.
107. Parry, C.M., et al., Typhoid fever. N Engl J Med, 2002. 347(22): p. 1770-82.
108. Nasronudin, Immunopatogenesismolekuler, Diagnosis dan Penatalaksanaan
Demam Tifoid Masa Kini, in Penyakit Infeksi di Indonesia Solusi Kini &
Mendatang2007, Surabaya: Airlangga University Press: Indonesia.
109. Pastoor, R., et al., Simple, rapid, and affordable point-of-care test for the
serodiagnosis of typhoid fever. Diagn Microbiol Infect Dis, 2008. 61(2): p. 129-34.
110. H. Gerardi, M. and M. C. Zimmerman, Wastewater Pathogens. 2005. 179 p.
111. Sudoyo, A.W., Buku Ajar Ilmu Penyakit Dalam. 2009, Indonesia: Jakarta: Interna
Publishing
112. TP, L. and H. SL, Typhoid fever, in Hunter's Tropical medicine and emerging
infectious diseases. 2000, Saunders: Philadelphia. p. 471–83.
113. Isselbacher, K.J., et al., Harrison's Principles of Internal Medicine. 2013, McGraw-
Hill Inc.: Singapore.
114. Tanto, C., et al., Kapita Selekta Kedokteran Jilid II. 2016, Media Aesculapius:
Jakarta. p. 721-723.
115. Prof. dr. Syarifuddin Wahid, P.D., Sp.PA (K), Sp.F and P.D. dr. Upik A. Miskad,
Sp.PA (K), IMUNOLOGI Lebih Mudah Dipahami. 2016: Brillian Internasional.
116. Abbas, A.K., A.H. Lichtman, and S. Pillai, Basic Immunology. Vol. 5th edition. 2016:
Elsevier.
117. Wahyuni, A. Hardjono, and P.H. Yamrewav, EKSTRAKSI KURKUMIN DARI KUNYIT.
SEMINAR NASIONAL REKAYASA KIMIA DAN PROSES 2004, 2004.
118. HATTA, M. and H.L. SMITS, DETECTION OF SALMONELLA TYPHI BY NESTED
POLYMERASE CHAIN REACTION IN BLOOD, URINE, AND STOOL SAMPLES. The
American Journal of Tropical Medicine and Hygiene, 2007. 76(1): p. 139-143.
119. Hospital, T.M.G. PRIMER BANK : PCR Primers for Gene Expression Detection and
Quantification. 2016 October 2016 [cited 2018 February 16]; Available from:
https://pga.mgh.harvard.edu/cgi-bin/primerbank/new_search2.cgi.
120. Yajima, T., et al., Quantitative reverse transcription-PCR assay of the RNA
component of human telomerase using the TaqMan fluorogenic detection system.
Clinical Chemistry, 1998. 44(12): p. 2441.