Oil Immersed Distribution Transformer HST Reduction using Vegetable Oils and ONAN Cooling

Today, the use of electricity sources is increasing as cities are growing. With the increasing use of mineral oils for transformers cooling in the distribution network, due to the problems encountered using these oils, an alternative fluid should be used inside the transformers instead of mineral oils. Therefore, mineral oils should be replaced with fluids that are more compatible with nature due to the environmental hazards and high costs. Hence, vegetable oils can be used as suitable alternatives for the mineral oils in transformers due to their low risk and the renewability. On the other hand, compared to the mineral oils that have a fire point of about 151 Celsius degrees, vegetable oils have fire points higher than 311 Celsius degrees. As a result, from this viewpoint, they are considered as harmless fluids. Vegetable oils are simply degraded in the nature, and due to their different chemical structures compared to the mineral oils, they can increase the life of the equipment. Besides, the most important point is that they improve the transformer cooling performance, in terms of thermal analysis. Thus, in this paper, the distribution transformer electromagnetic-thermal analysis and conjugate heat transfer, in presence of different types of vegetable oils, and different types of cores such as grain-oriented silicon steel, amorphous and vitroperm alloy are investigated. Afterwards, the obtained results, especially hot spot temperature, are compared with distribution transformer containing mineral oil. ANSYS software has also been used for simulations

Validation of Urinary Glycosaminoglycans in Iranian patients with Mucopolysaccharidase type I: The effect of urine sedimentation characteristics

How to Cite This Article:Abdi M, Khatami Sh, Hakhamaneshi MS, Alaei MR, Azadi NA, Zamanfar D, Taghikhani M.Validation of Urinary Glycosaminiglycans in Iranian Patients with Mucopolysaccharidose Type I: The Effect of Urine Sedimentation Characteristics. Iran J Child Neurol. 2014; 8(4):39-45. AbstractObjectiveThe first line-screening test for mucopolysaccharidosis is based on measurement of urinary glycosaminoglycans. The most reliable test for measurement of urine glycosaminoglycans is the 1,9-dimethyleneblue colorimetric assay. Biological markers are affected by ethnical factors, for this reason, the World Health Organization recommends that the diagnostic test characteristics should be used to determine results for different populations. This study determines the diagnostic value of 1,9-dimethyleneblue tests for diagnosis of mucopolysaccharidosis type I patients in Iran.Materials & Methods In addition to routine urine analysis, the qualitative and quantitative measurements of urine glucosaminoglycans were performed with the Berry spot test and 1,9-dimethyleneblue assay. Diagnostic values of the tests were determined using the ROC curve.ResultsUrine total glycosaminoglycans were significantly higher in male subjects than in female subjects. Glycosaminoglycan concentration was markedly decreased in specimens with elevated white blood cell and epithelial cells count. Using a cut-off level of 10.37 mg/g creatinine, sensitivity, and specificity were 100% and 97.22%, respectively, for a 1,9-dimethyleneblue colorimetric assay.ConclusionUrine glycosaminoglycans concentration significantly differs in our studied population. In addition to determine diagnostic validity of the 1,9-dimethyleneblue test, our results demonstrate the usefulness of measuring glycosaminoglycans for early screening of mucopolysaccharidosis type I Iran. ReferencesJackson RL, Busch SJ, Cardin AD. Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes. Physiological reviews. 1991 Apr;71(2):481-539.Ghaderi S. The biochemistry base of mucopolysaccharidoses and approach to. Genetics in the 3rd millennium. [Educational]. 2006;4(1):711-22.Mizumoto S, Ikegawa S, Sugahara K. Human genetic disorders caused by mutations in genes encoding biosynthetic enzymes for sulfated glycosaminoglycans. The Journal of biological chemistry. 2013 Apr 19;288(16):10953-61.Salbach J, Rachner TD, Rauner M, Hempel U, Anderegg U, Franz S, et al. Regenerative potential of glycosaminoglycans for skin and bone. Journal of molecular medicine (Berlin, Germany). 2012 Jun;90(6):625-35.Coppa GV, Catassi C, Gabrielli O, Giorgi PL, Dall’Amico R, Naia S, et al. Clinical application of a new simple method for the identification of mucopolysaccharidoses. Helvetica paediatrica acta. 1987 Jun;42(5-6):419-23.Fuller M, Meikle PJ, Hopwood JJ. Glycosaminoglycan degradation fragments in mucopolysaccharidosis I. Glycobiology. 2004 May;14(5):443-50.Fuller M, Rozaklis T, Ramsay SL, Hopwood JJ, Meikle PJ. Disease-specific markers for the mucopolysaccharidoses. Pediatric research. 2004 Nov;56(5):733-8.Blau N, Duran M, Gibson K. Laboratory Guide to the Methods in Biochemical Genetics. First edition ed: Springer-Verlag Berlin Heidelberg; 2008. pp287-324.Dorfman A, Matalon R. The Hurler and Hunter syndromes. The American journal of medicine. 1969 Nov;47(5):691-707.Fratantoni JC, Hall CW, Neufeld EF. Hurler and Hunter syndromes: mutual correction of the defect in cultured fibroblasts. Science (New York, NY. 1968 Nov 1;162(3853):570-2.Fratantoni JC, Hall CW, Neufeld EF. The defect in Hurler and Hunter syndromes. II. Deficiency of specific factors involved in mucopolysaccharide degradation. Proceedings of the National Academy of Sciences of the United States of America. 1969 Sep;64(1):360-6.Fratantoni JC, Neufeld EF, Uhlendorf BW, Jacobson CB. Intrauterine diagnosis of the hurler and hunter syndromes. The New England journal of medicine. 1969 Mar 27;280(13):686-8.Chamoles NA, Blanco MB, Gaggioli D, Casentini C. Hurler-like phenotype: enzymatic diagnosis in dried blood spots on filter paper. Clinical chemistry. 2001 Dec;47(12):2098-102.Nor A, Zabedah MY, Norsiah MD, Ngu LH, Suhaila AR. Separation of sulfated urinary glycosaminoglycans by high-resolution electrophoresis for isotyping of mucopolysaccharidoses in Malaysia. The Malaysian journal of pathology. 2010 Jun;32(1):35-42.De Muro P, Faedda R, Formato M, Re F, Satta A, Cherchi GM, et al. Urinary glycosaminoglycans in patients with systemic lupus erythematosus. Clinical and experimental rheumatology. 2001 Mar-Apr;19(2):125-30.Berry HK, Spinanger J. A paper spot test useful in study of Hurler’s syndrome. The Journal of laboratory and clinical medicine. 1960 Jan;55:136-8.Pennock CA, White F, Murphy D, Charles RG, Kerr H. Excess glycosaminoglycan excretion in infancy and childhood. Acta paediatrica Scandinavica. 1973 Sep;62(5):481-91.Berman ER, Vered J, Bach G. A reliable spot test for mucopolysaccharidoses. Clinical chemistry. 1971 Sep;17(9):886-90.Pennock CA. A review and selection of simple laboratory methods used for the study of glycosaminoglycan excretion and the diagnosis of the mucopolysaccharidoses. Journal of clinical pathology. 1976 Feb;29(2):111-23.Chan RW, Szeto CC. Advances in the clinical laboratory assessment of urinary sediment. Clinica chimica acta; international journal of clinical chemistry. 2004 Feb;340(1-2):67-78.Fogazzi GB, Garigali G. The clinical art and science of urine microscopy. Curr Opin Nephrol Hypertens. 2003 Nov;12(6):625-32.Berry HK. Screening for mucopolysaccharide disorders with the Berry spot test. Clinical biochemistry. 1987 Oct;20(5):365-71.de Jong JG, Hasselman JJ, van Landeghem AA, Vader HL, Wevers RA. The spot test is not a reliable screening procedure for mucopolysaccharidoses. Clinical chemistry. 1991 Apr;37(4):572-5.Mabe P, Valiente A, Soto V, Cornejo V, Raimann E. Evaluation of reliability for urine mucopolysaccharidosis screening by dimethylmethylene blue and Berry spot tests. Clinica chimica acta; international journal of clinical chemistry. 2004 Jul;345(1-2):135-40.Mahalingam K, Janani S, Priya S, Elango EM, Sundari RM. Diagnosis of mucopolysaccharidoses: how to avoid false positives and false negatives. Indian J Pediatr. 2004 Jan;71(1):29-32.de Jong JG, Wevers RA, Laarakkers C, Poorthuis BJ. Dimethyl methylene blue-based spectrophotometry of glycosaminoglycans in untreated urine: a rapid screening procedure for mucopolysaccharidoses. Clinical chemistry. 1989 Jul;35(7):1472-7.Panin G, Naia S, Dall’Amico R, Chiandetti L, Zachello F, Catassi C, et al. Simple spectrophotometric quantification of urinary excretion of glycosaminoglycan sulfates. Clinical chemistry. 1986 Nov;32(11):2073-6.Byers S, Rozaklis T, Brumfield LK, Ranieri E, Hopwood JJ. Glycosaminoglycan accumulation and excretion in the mucopolysaccharidoses: characterization and basis of a diagnostic test for MPS. Molecular genetics and metabolism. 1998 Dec;65(4):282-90.Carson NA, Neill DW. Metabolic abnormalities detected in a survey of mentally backward individuals in Northern Ireland. Archives of disease in childhood. 1962 Oct;37:505-13.Huang KC, Sukegawa K, Orii T. Screening test for urinary glycosaminoglycans and differentiation of various mucopolysaccharidoses. Clinica chimica acta; international journal of clinical chemistry. 1985 Sep 30;151(2):147-56.Chih-Kuang C, Shuan-Pei L, Shyue-Jye L, Tuen-Jen W. MPS screening methods, the Berry spot and acid turbidity tests, cause a high incidence of false-negative results in sanfilippo and morquio syndromes. Journal of clinical laboratory analysis. 2002;16(5):253-8.Gallegos-Arreola MP, Machorro-Lazo MV, Flores-Martinez SE, Zuniga-Gonzalez GM, Figuera LE, Gonzalez-Noriega A, et al. Urinary glycosaminoglycan excretion in healthy subjects and in patients with mucopolysaccharidoses. Archives of medical research. 2000 Sep-Oct;31(5):505-10.Piraud M, Maire I, Mathieu M. Pitfalls of screening for mucopolysaccharidoses by the dimethylmethylene blue test. Clinical chemistry. 1993 Jan;39(1):163-4.Whitley CB, Spielmann RC, Herro G, Teragawa SS. Urinary glycosaminoglycan excretion quantified by an automated semimicro method in specimens conveniently transported from around the globe. Molecular genetics and metabolism. 2002 Jan;75(1):56-64

Chitotriosidase Activity and Gene Polymorphism in Iranian Patients with Gaucher Disease and Sibling Carriers

How to Cite This Article: Mozafari H, Taghikhani M, Khatami Sh, Alaei MR, Vaisi-Raygani A, Rahimi Z. Chitotriosidase Activity and Gene Polymorphism in Iranian Patients with Gaucher Disease and Sibling Carriers. Iran J Child Neurol. Autumn 2016; 10(4):62-70.AbstractObjectiveChitotriosidase (CT) activity is a useful biomarker for diagnosis and monitoring of Gaucher disease (GD). Its application is limited by some variants in the CT gene. Two main polymorphisms are 24 bp duplication and G102S led to reduce CT activity. The aim of this study was to determine these variants influencing on plasma CT activity. Materials & MethodsBlood samples were collected from 33 patients with GD, 15 sibling carriers and 105 healthy individuals serving as controls. CT activity was measured using 4-methylumbelliferyl-β-D-N,N′,N″triacetylchitotrioside substrate in plasma samples. The CT genotypes of 24 bp duplication and G102S variants were determined using PCR and PCR-RFLP. ResultsUntreated GD patients had a significantly higher CT activity compared to treated patients (P = 0.021). In addition, chitotriosidase activity in carriers was higher rather than controls. Allele frequencies of 24 bp duplication in GD patients, sibling carriers and controls were 0.21, 0.266 and 0.29 and for G102S were 0.318, 0.366 and 0.219, respectively. Different G102S genotypes had not significant effect on CT activity. Chitotriosidase activity has a positive correlation with age in normal group, carriers, and negative correlation with hemoglobin in GD patients. Using cut-off level of 80.75 nmol/ml/h, sensitivity and specificity of CT activity were 93.9% and 100%, respectively. ConclusionChitotriosidase activity is a suitable biomarker for diagnosis and monitoring of GD. Determination of 24 bp duplication is helpful for more accurate monitoring the GD patient’s therapy. However, it seems that, specifying of the G102S polymorphism is not required for Iranian GD patients. References1. Bennett LL, Mohan D. Gaucher disease and its treatment  options. Ann Pharmacother 2013;47(9):1182-93.2. Shrestha B, Devgan A, Sharma M. Gaucher’s disease: rare presentation of a rare disease. J Child Neurol 2013;28(10):1296-8.3. Kanneganti M, Kamba A, Mizoguchi E. Role of chitotriosidase (chitinase 1) under normal and disease conditions. J Epithel Biol Pharmacol 2012;5:1-9.4. Adly AA, Ismail EA, Ibraheem TM. Macrophagederived soluble CD163 level in young patients with Gaucher disease: relation to phenotypes, disease severity and complications. Int Immunopharmacol 2015;24(2):416-22.5. Irún P, Alfonso P, Aznarez S, Giraldo P, Pocovi M.Chitotriosidase variants in patients with Gaucher disease.  Implications for diagnosis and therapeutic monitoring. Clin Biochem 2013;46(18):1804-7.6. Grace ME, Balwani M, Nazarenko I, Prakash- Cheng A, Desnick RJ. Type 1 Gaucher disease: null and hypomorphic novel chitotriosidase mutationsimplications for diagnosis and therapeutic monitoring. Hum Mutat 2007;28(9):866-73.7. Woo KH, Lee BH, Heo SH, Kim JM, Kim GH, Kim YM, et al. Allele frequency of a 24 bp duplication in exon 10 of the CHIT1 gene in the general Korean population and in Korean patients with Gaucher disease. J Hum Genet 2014;59(5):276-9.8. Wajner A, Michelin K, Burin MG, Pires RF, Pereira ML, Giugliani R, et al. Comparison between the biochemical properties of plasma chitotriosidase from normal individuals and from patients with Gaucher disease, GM1-gangliosidosis, Krabbe disease and heterozygotes for Gaucher disease. Clin Biochem 2007;40(5-6):365-9.9. Rosén C, Andersson CH, Andreasson U, Molinuevo JL, Bjerke M, Rami L, et al. Increased Levels of Chitotriosidase and YKL-40 in Cerebrospinal Fluid from Patients with Alzheimer’s Disease. Dement Geriatr Cogn Dis Extra 2014;31;4(2):297-304.10. Malaguarnera L. Chitotriosidase: the yin and yang. Cell Mol Life Sci 2006;63(24):3018-29.11. Pagliardini V, Pagliardini S, Corrado L, Lucenti A, Panigati L, Bersano E, et al. Chitotriosidase and lysosomal enzymes as potential biomarkers of disease progression in myotrophic lateral sclerosis: A survey clinic-based study. J Neurol Sci 2015;15;348(1-2):245-50.12. Fusetti F, von Moeller H, Houston D, Rozeboom HJ, Dijkstra BW, Boot RG, et al. Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins. J Biol Chem 2002;277:25537–25544.13. Sista RS, Wang T, Wu N, Graham C, Eckhardt A, Bali D, et al. Rapid assays for Gaucher and Hurler diseases in dried blood spots using digital microfluidics. Mol Genet Metab 2013;109(2): 218–220.14. Hollak CE, van Weely S, van Oers MH, Aerts JM. Marked elevation of plasma chitotriosidase activity. A novel hallmark of Gaucher disease. J Clin Invest 1994;93(3):1288–1292.15. Old JM, Higgs DR. Gene analysis. In: Weatherall DJ, editor. Methods in hematology. The thalassemias. Vol. 6. London: Churchill Livingstone; 1983. pp.74 – 101.16. Sinha S, Singh J, Jindal SK, Birbian N, Singla N. Association of 24 bp duplication of human CHIT1 gene with asthma in a heterozygous population of north India: a case-control study. Lung 2014;192(5):685-91.17. Manno N, Sherratt S, Boaretto F, Coico FM, Camus CE, Campos CJ, et al. High prevalence of chitotriosidase  deficiency in Peruvian Amerindians exposed to chitinbearing food and enteroparasites. Carbohydr Polym 2014;26;113:607-14.18. Adelino TE, Martins GG, Gomes AA, Torres AA, Silva DA, Xavier VD, et al. Biochemical and Molecular Chitotriosidase Profiles in Patients with Gaucher Disease Type 1 in Minas Gerais, Brazil: New Mutation in CHIT1 Gene. JIMD Rep 2013;9:85-91.19. van Dussen L, Hendriks EJ, Groener JE, Boot RG, Hollak CE, Aerts JM. Value of plasma chitotriosidase to assess non-neuronopathic Gaucher disease severity and progression in the era of enzyme replacement therapy. J Inherit Metab Dis 2014;37(6):991-1001.20. Weinreb NJ, Aggio MC, Andersson HC, Andria G, Charrow J, Clarke JT, et al. Gaucher disease type 1: revised recommendations on evaluations and monitoring for adult patients. Semin Hematol 2004;41:15–22.21. Czartoryska B, Tylki-Szymańska A, Górska D. Serum chitotriosidase activity in Gaucher patients on enzyme replacement therapy (ERT). Clin Biochem 1998;3(5):417-20.22. Arndt S1, Hobbs A, Sinclaire I, Lane AB. Chitotriosidase deficiency: a mutation update in an african population. JIMD Rep 2013;10:11-6.23. Lee P, Waalen J, Crain K, Smargon A, Beutler E. Human chitotriosidase polymorphisms G354R and A442V associated with reduced enzyme activity. Blood Cells Mol Dis 2007;39(3):353-60.24. Chien YH, Chen JH, Hwu WL. Plasma chitotriosidase activity and malaria. Clin Chim Acta 2005 ;353(1-2):215 25. Bussink AP, Verhoek M, Vreede J, Ghauharalivan der Vlugt K, Donker-Koopman WE, Sprenger RR, et al. Common G102S polymorphism in chitotriosidase differentially affects activity towards 4-methylumbelliferyl substrates. FEBS J 2009;276(19):5678-88.26. Aerts JM, Kallemeijn WW, Wegdam W, Joao Ferraz M, van Breemen MJ, Dekker N, et al. Biomarkers in the diagnosis of lysosomal storage disorders: proteins, lipids, and inhibodies. J Inherit Metab Dis 2011;34(3):605-19.27. Giraldo P, Cenarro A, Alfonso P, Pérez-Calvo JI, Rubio- Félix D, Giralt M, et al. Chitotriosidase genotype and plasma activity in patients type 1 Gaucher’s disease and their relatives (carriers and non carriers). Haematologica 2001;86(9):977-84.28. Pocovi M, Cenarro A, Civeira F, Torralba MA, Perez- Calvo JI, Mozas P, et al. Beta-glucocerebrosidase gene locus as a link for Gaucher’s disease and familial hypoalpha- lipoproteinaemia. Lancet 1998;351(9120):1919-23.29. Fluiter K, van der Westhuijzen DR, van Berkel TJ. In vitro regulation of scavenger receptor BI and the selective uptake of high density lipoprotein choles-teryl esters in rat liver parenchymal and Kupffer cells. J Biol Chem 1998; 273:8434-8.30. Ries M, Schaefer E, Lührs T, Mani L, Kuhn J, Vanier MT, et al. Critical assessment of chitotriosidase analysis in the rational laboratory diagnosis of children with Gaucher disease and Niemann-Pick disease type A/B and C. J Inherit Metab Dis 2006;29:647–652.31. Kurt I, Abasli D, Cihan M, Serdar MA, Olgun A, Saruhan E, et al. Chitotriosidase Levels in Healthy Elderly Subjects. Ann N Y Acad Sci 2007;1100:185-8.32. Tamanaha P, D’Almeida V, Calegare BF, Tomita LY, Bittencourt LR, Tufik S. 24 bp duplication of CHIT1 gene and determinants of human chitotriosidase activity among participants of EPISONO, a population-based cross-sectional study, São Paulo, Brazil. Clin Biochem 2013;46(12):1084-8.33. Dodelson de Kremer R, Paschini de Capra A, Angaroni CJ, Giner de Ayala A. Plasma chitotriosidase activity in Argentinian patients with Gaucher disease, various lysosomal diseases and other inherited metabolic disorders. Medicina (B Aires). 1997;57(6):677-84.34. Goldim MP, Garcia Cda S, de Castilhos CD, Daitx VV, Mezzalira J, Breier AC, et al. Screening of high-risk Gaucher disease patients in Brazil using miniaturized dried blood spots and leukocyte techniques. Gene 2012;508(2):197-8.

Understanding the polydisperse behavior of asphaltenes during precipitation

h i g h l i g h t s The PC-SAFT equation-of-state is used to study asphaltene phase behavior. The effect of asphaltene polydispersity on asphaltene phase behavior is studied. Results of monodisperse and polydisperse asphaltenes modeling are compared. A wide range of crude oils are considered for the study. An explanation for the observed behavior is provided based on Flory-Huggins theory. a r t i c l e i n f o b s t r a c t Asphaltenes are a polydisperse fraction of the crude oil, the phase behavior of which is significantly affected by the changes in pressure, temperature and composition. The focus of this study is to model the polydisperse asphaltenes' precipitation onset condition and the amount of precipitate from solvent-diluted crude oils using the Perturbed Chain form of the Statistical Associating Fluid Theory (PC-SAFT) over a wide range of crude oil density. Heavy oil and bitumen production can involve diluting with paraffinic solvents. Different fractions of the polydisperse asphaltenes thus precipitated are predicted and when compared to the experimental data show a remarkable matching for different solvents. A comparison of monodisperse and polydisperse modeling is also performed. This work illustrates the successful application of PC-SAFT for predicting the phase behavior of polydisperse asphaltenes and in particular from heavy oil and bitumen

Virulence factors of Helicobacter pylori vacA increase markedly gastric mucosal TGF-beta 1 mRNA expression in gastritis patients

Objective: Helicobacter pylori (H. pylori) infection is the main cause of gastric inflammation. Regulatory T cells (Treg cells) suppress the activation and proliferation of antigen-specific T cells and mediate immunologic tolerance. TGF-beta 1 was shown to be secreted in a subset of Treg cells known as `Th3 cells'. These cells have not been sufficiently studied in context to H. pylon-induced inflammation in human gastric mucosa. In this study we therefore, aimed to investigate the expression of TGF-beta 1 in the context of H. pylori colonization in chronic gastritis, to examine the relationship between it and histopathologic findings and to compare it with virulence factors. Patients and methods: Total RNA was extracted from gastric biopsies of 48 H. pylori-infected patients and 38 H. pylori-negative patients with gastritis. Mucosal TGF-beta 1 mRNA expression in H. pylori-infected and uninfected gastric biopsies was determined by real-time PCR. Presence of vacA, cagA, iceA, babA2 and oipA virulence factors was evaluated using PCR. Results: TGF-beta 1 mRNA expression was significantly increased in biopsies of H. pylori-infected patients compared to H. pylori-uninfected patients. There was association between virulence factors and TGF-beta 1 mRNA expression. TGF-beta 1 mRNA expression in mucosa was significantly higher in patients with vacA s1 and s1m1. Conclusions: TGF-beta 1 may play an important role in the inflammatory response and promote the chronic and persistent inflammatory changes in the gastric. This may ultimately influence the outcome of H. pylon-associated diseases that arise within the context of gastritis and vacA may suffice to induce expression of TGF-beta 1 mRNA. (C) 2014 Elsevier Ltd. All rights reserved

Preparation of monoclonal antibodies against mannosylated lipoarabinomannan (ManLAM), a surface antigen of BCG vaccine produced in Iran

Background: Bacille Calmette–Guerin (BCG) vaccine is the only vaccine that is used against Mycobacterium tuberculosis, but its efficacy is limited in mycobacterium-endemic regions. One of the major antigens present on the cell envelope of the vaccine that suppresses the immune system is mannosylated lipoarabinomannan (ManLAM). Materials and Methods: In this study, we immunized 4-week-old mice with sonicated BCG vaccine injected intraperitoneally two times at an interval of 2 weeks and with ManLAM antigen injected intravenously and then extracted the spleen cells of the immunized mice. They were fused with SP2/0 myeloma cells. Results: Five cell line clones producing antibody against ManLAM antigens were prepared and each clone was tested for immunoreactivity against sonicated BCG and purified ManLAM by enzyme-linked immunosorbent assay (ELISA) and immunoblotting. The clones designated H13F33E11 and H23D91G4 reacted strongly with ManLAM. Immunoblotting using monoclonal antibodies (MAbs) H13F33E11 and H23D91G4 showed that these MAbs bind to ManLAM with a molecular weight of 35 kDa. Conclusions: In this study, we produced a monoclonal antibody of immunoglobulin G3 (IgG3) subclass. This MAb can be used for purification of ManLAM in culture media and detection of the antigen in patient's urine and for increasing the efficacy of BCG vaccine