Toll様受容体2

関: Toll-like receptor 2

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/08/05 16:29:35」(JST)

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Toll-like receptor 2 also known as TLR2 is a protein that in humans is encoded by the TLR2 gene.^[3] TLR2 has also been designated as CD282 (cluster of differentiation 282). TLR2 is one of the toll-like receptors and plays a role in the immune system. TLR2 is a membrane protein, a receptor, which is expressed on the surface of certain cells and recognizes foreign substances and passes on appropriate signals to the cells of the immune system.

Function

The protein encoded by this gene is a member of the Toll-like receptor (TLR) family, which plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) that are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. This gene is expressed most abundantly in peripheral blood leukocytes, and mediates host response to Gram-positive bacteria^[4] and yeast via stimulation of NF-κB.^[5]

In the intestine, TLR2 regulates the expression of CYP1A1,^[6] which is a key enzyme in detoxication of carcinogenic polycyclic aromatic hydrocarbons such as benzo(a)pyrene.^[7]

Background

The immune system recognizes foreign pathogens and eliminates them. This occurs in several phases. In the early inflammation phase, the pathogens are recognized by antibodies that are already present (innate or acquired through prior infection; see also cross-reactivity). Immune-system components (e.g. complement) are bound to the antibodies and kept near, in reserve to disable them via phagocytosis by scavenger cells (e.g. macrophages). Dendritic cells are likewise capable of phagocytizing but do not do it for the purpose of direct pathogen elimination. Rather, they infiltrate the spleen and lymph nodes, and each presents components of an antigen there, as the result of which specific antibodies are formed that recognize precisely that antigen.

These newly formed antibodies would arrive too late in an acute infection, however, so what we think of as "immunology" constitutes only the second half of the process. Because this phase would always start too late to play an essential role in the defense process, a faster-acting principle is applied ahead of it, one that occurs only in forms of life that are phylogenetically more highly developed.

What are called pattern-recognition receptors come into play here. This refers to receptors that recognize the gross, primarily structural features of molecules not innate to the host organism. These include, for example, lipids with a totally different basic chemical structure. Such receptors are bound directly to cells of the immune system and cause immediate activation of their respective nonspecific immune cells.

A prime example of such a foreign ligand is bacterial endotoxin, whose effects have been known for generations. When it enters the bloodstream it causes systematic activation of the early-phase response, with all the side effects of septic shock. This is known in the laboratory as the Shwartzman phenomenon. The intended effect is to mobilize the organism for combat, so to speak, and eliminate most of the pathogens.

Mechanism

As a membrane surface receptor, TLR2 recognizes many bacterial, fungal, viral, and certain endogenous substances. In general, this results in the uptake (internalization, phagocytosis) of bound molecules by endosomes/phagosomes and in cellular activation; thus such elements of innate immunity as macrophages, PMNs and dendritic cells assume functions of nonspecific immune defense, B1a and MZ B cells form the first antibodies, and specific antibody formation gets started in the process. Cytokines participating in this include tumor necrosis factor-alpha (TNF-α) and various interleukins (IL-1α, IL-1β, IL-6, IL-8, IL-12). Before the TLRs were known, several of the substances mentioned were classified as modulins. Due to the cytokine pattern, which corresponds more closely to T_h1, an immune deviation is seen in this direction in most experimental models, away from T_h2 characteristics. Conjugates are being developed as vaccines or are already being used without a priori knowledge.

A peculiarity first recognized in 2006 is the expression of TLR2 on Tregs (a type of T cell), which experience both TCR-controlled proliferation and functional inactivation. This leads to disinhibition of the early inflammation phase and of specific antibody formation. Following a reduction in pathogen count, many pathogen-specific Tregs are present that, now without a TLR2 signal, become active and inhibit the specific and inflammatory immune reactions (see also TNF-β, IL-10). Older literature that ascribes a direct immunity-stimulating effect via TLR2 to a given molecule must be interpreted in light of the fact that the TLR2 knockouts employed typically have very few Tregs.

Functionally relevant polymorphisms are reported that cause functional impairment and thus, in general, reduced survival rates, in particular in infections/sepsis with Gram-positive bacteria.

Signal transduction is depicted under Toll-like receptor.

Expression

TLR2 is expressed on microglia, Schwann cells, monocytes, macrophages, dendritic cells, polymorphonuclear leukocytes (PMNs or PMLs), B cells (B1a, MZ B, B2), and T cells, including Tregs (CD4+CD25+ regulatory T cells). In some cases, it occurs in a heterodimer (combination molecule), e.g., paired with TLR-1 or TLR-6. TLR2 is also found in the epithelia of air passages, pulmonary alveoli, renal tubules, and the Bowman's capsules in renal corpuscles. TLR2 is also expressed by intestinal epithelial cells and subsets of lamina propria mononuclear cells in the gastrointestinal tract ^[8] . In the skin, it is found on keratinocytes and sebaceous glands; spc1 is induced here, allowing a bactericidal sebum to be formed.

Agonists

The following ligands have been reported to be agonists of the toll-like receptor 2:

Agonist	Organism
Lipoteichoic acid	Gram-positive bacteria
atypical LPS	Leptospirosis and Porphyromonas gingivalis
MALP-2 and MALP-404 (lipoproteins)	Mycoplasma
-	Chlamydophila pneumoniae
OspA	Borrelia burgdorferi (Lyme disease)
Porin	Neisseria meningitidis, Haemophilus influenzae
Antigen mixtures	Propionibacterium acnes
LcrV	Yersinia
Lipomannan	Mycobacterium: Mycobacterium tuberculosis
GPI anchor	Trypanosoma cruzi
Lysophosphatidylserine	Schistosoma mansoni
Lipophosphoglycan (LPG)	Leishmania major
Glycophosphatidylinositol (GPI)	Plasmodium falciparum
Zymosan (a beta-glucan)	Saccharomyces cerevisiae
-	Malassezia (commensal yeast)
Antigen mixtures	Aspergillus fumigatus, Candida albicans
hsp60, as peptide transporter and adjuvant for antigen presentation	-
Glycoprotein (gH/gL, gB)^[9]	Herpes simplex virus
-	Varicella zoster virus
-	Cytomegalovirus (CMV)
Hemagglutinin	Measles

Interactions

Protein-protein interactions

TLR 2 has been shown to interact with TLR 1^[10] and TOLLIP.^[11]

Protein-ligand interactions

TLR2 resides on the plasma membrane where it responds to lipid-containing PAMPs such as lipoteichoic acid and di- and tri-acylated cysteine-containing lipopeptides. It does this by forming dimeric complexes with either TLR 1 or TLR6 on the plasma membrane.^[12] TLR2 interactions with malarial glycophosphatidylinositols of Plasmodium falciparum was shown^[13] and a detailed structure of TLR–GPI interactions was computationally predicted.^[14]

Gene polymorphisms

Various single nucleotide polymorphisms (SNPs) of the TLR2 have been identified ^[15] and for some of them an association with faster progression and a more severe course of sepsis in critically ill patients was reported.^[16] No association with occurrence of severe staphylococcal infection was found.^[17]

References

^ "Human PubMed Reference:".
^ "Mouse PubMed Reference:".
^ Rock FL, Hardiman G, Timans JC, Kastelein RA, Bazan JF (January 1998). "A family of human receptors structurally related to Drosophila Toll". Proceedings of the National Academy of Sciences of the United States of America. 95 (2): 588–93. PMC 18464 . PMID 9435236. doi:10.1073/pnas.95.2.588.
^ Borrello S, Nicolò C, Delogu G, Pandolfi F, Ria F (2011). "TLR2: a crossroads between infections and autoimmunity?". International Journal of Immunopathology and Pharmacology. 24 (3): 549–56. PMID 21978687.
^ "Entrez Gene: TLR2".
^ Do KN, Fink LN, Jensen TE, Gautier L, Parlesak A (2012). "TLR2 controls intestinal carcinogen detoxication by CYP1A1". PloS One. 7 (3): e32309. PMC 3307708 . PMID 22442665. doi:10.1371/journal.pone.0032309.
^ Uno S, Dalton TP, Dragin N, Curran CP, Derkenne S, Miller ML, Shertzer HG, Gonzalez FJ, Nebert DW (April 2006). "Oral benzo[a]pyrene in Cyp1 knockout mouse lines: CYP1A1 important in detoxication, CYP1B1 metabolism required for immune damage independent of total-body burden and clearance rate". Molecular Pharmacology. 69 (4): 1103–14. PMID 16377763. doi:10.1124/mol.105.021501.
^ Cario E (Nov 2008). "Barrier-protective function of intestinal epithelial Toll-like receptor 2". Mucosal Immunology. Suppl 1: S62–6. PMID 19079234. doi:10.1038/mi.2008.47.
^ Leoni, Valerio; Gianni, Tatiana; Salvioli, Stefano; Campadelli-Fiume, Gabriella (2012-06-15). "Herpes Simplex Virus Glycoproteins gH/gL and gB Bind Toll-Like Receptor 2, and Soluble gH/gL Is Sufficient To Activate NF-κB". Journal of Virology. 86 (12): 6555–6562. ISSN 0022-538X. PMC 3393584 . PMID 22496225. doi:10.1128/JVI.00295-12.
^ Takeuchi O, Sato S, Horiuchi T, Hoshino K, Takeda K, Dong Z, Modlin RL, Akira S (July 2002). "Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins". Journal of Immunology. 169 (1): 10–4. PMID 12077222. doi:10.4049/jimmunol.169.1.10.
^ Zhang G, Ghosh S (March 2002). "Negative regulation of toll-like receptor-mediated signaling by Tollip". The Journal of Biological Chemistry. 277 (9): 7059–65. PMID 11751856. doi:10.1074/jbc.M109537200.
^ Botos I, Segal DM, Davies DR (April 2011). "The structural biology of Toll-like receptors". Structure. 19 (4): 447–59. PMC 3075535 . PMID 21481769. doi:10.1016/j.str.2011.02.004.
^ Zhu J, Krishnegowda G, Li G, Gowda DC (July 2011). "Proinflammatory responses by glycosylphosphatidylinositols (GPIs) of Plasmodium falciparum are mainly mediated through the recognition of TLR2/TLR1". Experimental Parasitology. 128 (3): 205–11. PMC 3100359 . PMID 21439957. doi:10.1016/j.exppara.2011.03.010.
^ Durai P, Govindaraj RG, Choi S (December 2013). "Structure and dynamic behavior of Toll-like receptor 2 subfamily triggered by malarial glycosylphosphatidylinositols of Plasmodium falciparum". The FEBS Journal. 280 (23): 6196–212. PMID 24090058. doi:10.1111/febs.12541.
^ Schröder NW, Schumann RR (March 2005). "Single nucleotide polymorphisms of Toll-like receptors and susceptibility to infectious disease". The Lancet. Infectious Diseases. 5 (3): 156–64. PMID 15766650. doi:10.1016/S1473-3099(05)01308-3.
^ Nachtigall I, Tamarkin A, Tafelski S, Weimann A, Rothbart A, Heim S, Wernecke KD, Spies C (February 2014). "Polymorphisms of the toll-like receptor 2 and 4 genes are associated with faster progression and a more severe course of sepsis in critically ill patients". The Journal of International Medical Research. 42 (1): 93–110. PMID 24366499. doi:10.1177/0300060513504358.
^ Moore CE, Segal S, Berendt AR, Hill AV, Day NP (November 2004). "Lack of association between Toll-like receptor 2 polymorphisms and susceptibility to severe disease caused by Staphylococcus aureus". Clinical and Diagnostic Laboratory Immunology. 11 (6): 1194–7. PMC 524778 . PMID 15539529. doi:10.1128/CDLI.11.6.1194-1197.2004.

UpToDate Contents

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1. Toll様受容体：疾患および治療における役割 toll like receptors roles in disease and therapy
2. 結核の免疫学 immunology of tuberculosis
3. 痛風性関節炎の病態生理 pathophysiology of gouty arthritis
4. 尋常性ざ瘡の病因、臨床症状、および診断 pathogenesis clinical manifestations and diagnosis of acne vulgaris
5. 敗血症の病態生理 pathophysiology of sepsis

English Journal

Soluble Toll-like receptor 2 is a biomarker for sepsis in critically ill patients with multi-organ failure within 12 h of ICU admission.

Holst B1, Szakmany T2,3,4, Raby AC5, Hamlyn V1,6, Durno K1, Hall JE1, Labéta MO7.
Intensive care medicine experimental.Intensive Care Med Exp.2017 Dec;5(1):2. doi: 10.1186/s40635-016-0116-z. Epub 2017 Jan 13.
PMID 28092080

Topical application of the anti-microbial chemical triclosan induces immunomodulatory responses through the S100A8/A9-TLR4 pathway.

Marshall NB1, Lukomska E1, Nayak AP1, Long CM1,2, Hettick JM1, Anderson SE1.
Journal of immunotoxicology.J Immunotoxicol.2017 Dec;14(1):50-59. doi: 10.1080/1547691X.2016.1258094.
PMID 28121465

Biocompatibility of Liposome Nanocarriers in the Rat Inner Ear After Intratympanic Administration.

Zou J1,2, Feng H3,4, Sood R5, Kinnunen PKJ5, Pyykko I3.
Nanoscale research letters.Nanoscale Res Lett.2017 Dec;12(1):372. doi: 10.1186/s11671-017-2142-5. Epub 2017 May 25.
PMID 28549377

Japanese Journal

Contribution of Toll-Like Receptor 2 to the Innate Response against Staphylococcus aureus Infection in Mice

Yimin,Kohanawa Masashi,Zhao Songji,Ozaki Michitaka,Haga Sanae,Nan Guangxian,Kuge Yuji,Tamaki Nagara
Plos one 8(9), e74287, 2013-09-13
… The function of TLRs, specifically TLR2, during S. … In this study, we investigated the extent to which TLR2 contributes to the host innate response against the bacterial infection using TLR2-deficient mice. … aureus resulted in all TLR2-deficient mice dying within 4 d, along with a high bacterial burden in the livers. …
NAID 120005347005

Xanthoceraside Inhibits Pro-inflammatory Cytokine Expression in Aβ₂₅₋₃₅/IFN-γ-Stimulated Microglia Through the TLR2 Receptor, MyD88, Nuclear Factor-κB, and Mitogen-Activated Protein Kinase Signaling Pathways

Qi Yue,Zou Li-Bo,Wang Li-Hua [他]
Journal of pharmacological sciences 122(4), 305-317, 2013-08
NAID 40019753486

TLR3-mediated apoptosis and activation of phosphorylated Akt in the salivary gland epithelial cells of primary Sjögren's syndrome patients

Nakamura Hideki,Horai Yoshiro,Suzuki Takahisa,Okada Akitomo,Ichinose Kunihiro,Yamasaki Satoshi,Koji Takehiko,Kawakami Atsushi
Rheumatology International 33(2), 441-450, 2013-02
… Expression of TLR2 and TLR3 with pAkt was observed in cultured SGECs after 24-h stimulation with each ligand. …
NAID 120005230844

「Toll様受容体2」

TLR2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1FYW, 1FYX, 1O77, 2Z7X, 2Z80
Identifiers
Aliases	TLR2, CD282, TIL4, toll like receptor 2
External IDs	OMIM: 603028 MGI: 1346060 HomoloGene: 20695 GeneCards: TLR2
Gene ontology
Molecular function	• signaling pattern recognition receptor activity; • lipopolysaccharide binding; • Toll-like receptor binding; • triacyl lipopeptide binding; • protein binding; • peptidoglycan binding; • protein heterodimerization activity; • lipopolysaccharide receptor activity; • transmembrane signaling receptor activity; • receptor activity; • lipopeptide binding;
Cellular component	• cytoplasm; • integral component of membrane; • phagocytic vesicle membrane; • Golgi apparatus; • membrane; • intrinsic component of plasma membrane; • plasma membrane; • Toll-like receptor 1-Toll-like receptor 2 protein complex; • integral component of plasma membrane; • membrane raft; • cytoplasmic vesicle; • cell projection; • cell surface; • cell body;
Biological process	• interleukin-10 production; • positive regulation of interferon-beta production; • defense response to Gram-positive bacterium; • positive regulation of interleukin-18 production; • positive regulation of toll-like receptor signaling pathway; • toll-like receptor TLR1:TLR2 signaling pathway; • positive regulation of inflammatory response; • cellular response to bacterial lipopeptide; • positive regulation of interleukin-12 production; • immune system process; • detection of diacyl bacterial lipopeptide; • regulation of cytokine secretion; • cellular response to diacyl bacterial lipopeptide; • I-kappaB phosphorylation; • positive regulation of nitric-oxide synthase biosynthetic process; • MyD88-dependent toll-like receptor signaling pathway; • cellular response to triacyl bacterial lipopeptide; • detection of triacyl bacterial lipopeptide; • positive regulation of Wnt signaling pathway; • positive regulation of gene expression; • cellular response to lipoteichoic acid; • positive regulation of NF-kappaB transcription factor activity; • immune response; • positive regulation of interleukin-8 production; • positive regulation of interleukin-6 production; • positive regulation of tumor necrosis factor production; • cytokine secretion involved in immune response; • positive regulation of chemokine production; • positive regulation of NF-kappaB import into nucleus; • innate immune response; • inflammatory response; • toll-like receptor TLR6:TLR2 signaling pathway; • response to molecule of bacterial origin; • signal transduction; • positive regulation of transcription from RNA polymerase II promoter; • apoptotic process; • response to lipopolysaccharide; • response to progesterone; • toll-like receptor signaling pathway; • response to insulin; • central nervous system myelin formation; • nitric oxide metabolic process; • response to fatty acid; • leukotriene metabolic process; • toll-like receptor 2 signaling pathway; • positive regulation of oligodendrocyte differentiation; • response to bacterial lipoprotein; • negative regulation of cell proliferation; • response to toxic substance; • response to hypoxia; • positive regulation of interleukin-10 production; • lipopolysaccharide-mediated signaling pathway; • microglial cell activation;
	Sources:Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	7097
	24088
	ENSG00000137462
	ENSMUSG00000027995
	O60603
	Q9QUN7
NM_003264; NM_001318787; NM_001318789; NM_001318790; NM_001318791;
	NM_001318793; NM_001318795; NM_001318796
	NM_011905
NP_001305716; NP_001305718; NP_001305719; NP_001305720; NP_001305722;
	NP_001305724; NP_001305725; NP_003255
	NP_036035
	Wikidata
View/Edit Human	View/Edit Mouse

　　[★]

英: Toll-like receptor 2、TLR2
関: Toll様レセプター2

「TL」

　　[★]

[1] "Human PubMed Reference:".

[2] "Mouse PubMed Reference:".

[pmid9435236-3] Rock FL, Hardiman G, Timans JC, Kastelein RA, Bazan JF (January 1998). "A family of human receptors structurally related to Drosophila Toll". Proceedings of the National Academy of Sciences of the United States of America. 95 (2): 588–93. PMC 18464 . PMID 9435236. doi:10.1073/pnas.95.2.588.

[pmid21978687-4] Borrello S, Nicolò C, Delogu G, Pandolfi F, Ria F (2011). "TLR2: a crossroads between infections and autoimmunity?". International Journal of Immunopathology and Pharmacology. 24 (3): 549–56. PMID 21978687.

[entrez-5] "Entrez Gene: TLR2".

[pmid22442665-6] Do KN, Fink LN, Jensen TE, Gautier L, Parlesak A (2012). "TLR2 controls intestinal carcinogen detoxication by CYP1A1". PloS One. 7 (3): e32309. PMC 3307708 . PMID 22442665. doi:10.1371/journal.pone.0032309.

[pmid16377763-7] Uno S, Dalton TP, Dragin N, Curran CP, Derkenne S, Miller ML, Shertzer HG, Gonzalez FJ, Nebert DW (April 2006). "Oral benzo[a]pyrene in Cyp1 knockout mouse lines: CYP1A1 important in detoxication, CYP1B1 metabolism required for immune damage independent of total-body burden and clearance rate". Molecular Pharmacology. 69 (4): 1103–14. PMID 16377763. doi:10.1124/mol.105.021501.

[pmid19079234-8] Cario E (Nov 2008). "Barrier-protective function of intestinal epithelial Toll-like receptor 2". Mucosal Immunology. Suppl 1: S62–6. PMID 19079234. doi:10.1038/mi.2008.47.

[9] Leoni, Valerio; Gianni, Tatiana; Salvioli, Stefano; Campadelli-Fiume, Gabriella (2012-06-15). "Herpes Simplex Virus Glycoproteins gH/gL and gB Bind Toll-Like Receptor 2, and Soluble gH/gL Is Sufficient To Activate NF-κB". Journal of Virology. 86 (12): 6555–6562. ISSN 0022-538X. PMC 3393584 . PMID 22496225. doi:10.1128/JVI.00295-12.

[pmid12077222-10] Takeuchi O, Sato S, Horiuchi T, Hoshino K, Takeda K, Dong Z, Modlin RL, Akira S (July 2002). "Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins". Journal of Immunology. 169 (1): 10–4. PMID 12077222. doi:10.4049/jimmunol.169.1.10.

[pmid11751856-11] Zhang G, Ghosh S (March 2002). "Negative regulation of toll-like receptor-mediated signaling by Tollip". The Journal of Biological Chemistry. 277 (9): 7059–65. PMID 11751856. doi:10.1074/jbc.M109537200.

[pmid21481769-12] Botos I, Segal DM, Davies DR (April 2011). "The structural biology of Toll-like receptors". Structure. 19 (4): 447–59. PMC 3075535 . PMID 21481769. doi:10.1016/j.str.2011.02.004.

[pmid21439957-13] Zhu J, Krishnegowda G, Li G, Gowda DC (July 2011). "Proinflammatory responses by glycosylphosphatidylinositols (GPIs) of Plasmodium falciparum are mainly mediated through the recognition of TLR2/TLR1". Experimental Parasitology. 128 (3): 205–11. PMC 3100359 . PMID 21439957. doi:10.1016/j.exppara.2011.03.010.

[pmid24090058-14] Durai P, Govindaraj RG, Choi S (December 2013). "Structure and dynamic behavior of Toll-like receptor 2 subfamily triggered by malarial glycosylphosphatidylinositols of Plasmodium falciparum". The FEBS Journal. 280 (23): 6196–212. PMID 24090058. doi:10.1111/febs.12541.

[pmid_.3D_15766650-15] Schröder NW, Schumann RR (March 2005). "Single nucleotide polymorphisms of Toll-like receptors and susceptibility to infectious disease". The Lancet. Infectious Diseases. 5 (3): 156–64. PMID 15766650. doi:10.1016/S1473-3099(05)01308-3.

[pmid_.3D_24366499-16] Nachtigall I, Tamarkin A, Tafelski S, Weimann A, Rothbart A, Heim S, Wernecke KD, Spies C (February 2014). "Polymorphisms of the toll-like receptor 2 and 4 genes are associated with faster progression and a more severe course of sepsis in critically ill patients". The Journal of International Medical Research. 42 (1): 93–110. PMID 24366499. doi:10.1177/0300060513504358.

[pmid_.3D_15539529-17] Moore CE, Segal S, Berendt AR, Hill AV, Day NP (November 2004). "Lack of association between Toll-like receptor 2 polymorphisms and susceptibility to severe disease caused by Staphylococcus aureus". Clinical and Diagnostic Laboratory Immunology. 11 (6): 1194–7. PMC 524778 . PMID 15539529. doi:10.1128/CDLI.11.6.1194-1197.2004.

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1-50	CD1 a-c 1A 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51-100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101-150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151-200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201-250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251-300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301-350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

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TLR2