Investigation of lectin binding on rabbit spleen cell membrane infected with Proteus vulgaris

Year 2024, Volume: 33 Issue: 2, 109 - 122

Maryam Dıanı , Hakan Eskizengin , Mohammad Nima Badalı , Nursel Gül

https://doi.org/10.53447/communc.1424347

Abstract

This study investigated the effects of Proteus vulgaris OX19 infection on the carbohydrate composition of spleen cell membranes in New Zealand adult male rabbits. Rabbits were injected with increasing doses of P. vulgaris OX19 (0.5 ml, 1 ml, 2 ml, 4 ml, 5 ml) at five-day intervals over the course of one month. Following the treatment period, spleen tissues were collected from both the control and infected groups. Tissue sections were stained using the Avidin-Biotin-Peroxidase method with five different lectins: Concavalia ensiformis (Con A), Arachis hypogaea agglutinin (PNA), Bauhinia purpurea agglutinin (BPA), Griffonia simplicifolia I (GS-I), and Ulex europaeus agglutinin I (UEA-I). The stained sections were examined by light microscopy to evaluate lectin binding. Among the lectins used, Con A showed strong binding (+++) to spleen cell membranes of the Proteus-infected group, while moderate binding (++) was observed in the control group. UEA-I exhibited weak binding in the control group but demonstrated moderate binding in the Proteus-infected group. In contrast, PNA, BPA, and GS-I exhibited strong binding (+++) to spleen cell membranes in the control group and moderate binding (++) in the infected group. These findings suggest that P. vulgaris OX19 infection induces alterations in the carbohydrate moieties of glycoproteins and glycolipids in the spleen cell membranes of infected rabbits. It is hypothesized that P. vulgaris modifies the terminal carbohydrates of glycoproteins and/or glycolipids in spleen cell membranes, contributing to the observed changes in lectin binding patterns.

Keywords

Proteus vulgaris, rabbit, spleen, lectins, histochemical staining, light microscopy

References

• Sanders, W. E., Sanders, C. C., Enterobacter spp.: pathogens poised to flourish at the turn of the century. Clinical Microbiology Reviews, 10 (2) (1997), 220-41. https://doi.org/10.1128/cmr.10.2.220
• Stock, I., Grüger, T., Wiedemann, B., Natural antibiotic susceptibility of strains of the Enterobacter cloacae complex. International Journal of Antimicrobial Agents, 18 (6) (2001), 537-45. https://doi.org/10.1016/s0924-8579(01)00463-0
• McLean, R. J., Nickel, J. C., Cheng, K. J., Costerton, J. W., The ecology and pathogenicity of urease-producing bacteria in the urinary tract. Critical Reviews in Microbiology, 16 (1) (1988), 37-79. https://doi.org/10.3109/10408418809104467
• Martinko, M. J., Madigan, M. T., Brock Mikroorganizmaların Biyolojisi, Palme Yayıncılık, Ankara, 2010.
• Durak, Y., Kır, M., Özkalp, B., Aladağ, M. O., Çeşitli Klinik Materyallerden İzole Edilen Gram Negatif ve Gram Pozitif Bakterilerin Ofloxacin’e Karşı Duyarlılıklarının Araştırılması. Ulusal Biyoteknoloji Kongresi, 63 (1) (2005), 17-14.
• Vurgun, N., Ece, A., Çetinkaya, Z., Zeki, A., Balkan, C., Çocuk idrar yolu enfeksiyonlarında etken mikroorganizmalar ve antibiyotik duyarlılıkları. Medical Journal of Süleyman Demirel University, 3 (3) (1996), 77-81.
• Bozkurt, H., Güdücüoğlu, H., Kurtoğlu, M. G., Körkoca, H., Çiftçi, İ. H., Aygül, K., Berktaş, M., Klinik örneklerden izole edilen Proteus vulgaris suşlarının antimikrobiyal ajanlara duyarlılıkları. Van Tıp Dergisi, 12 (2) (2005), 145-148.
• Özkanlar, Y., Şahal, M., Kibar, M., Özkök, S., Köpeklerde Escherichia coli ve Proteus mirabilis ile oluşturulan aşağı üriner sistem enfeksiyonu ve vezikoüreteral refluksla ilişkisi. Ankara Üniversitesi Veteriner Fakültesi Dergisi, 52 (2005), 171-178.
• Sharon, N., Lectins. Scientific American Magazine, 236 (6) (1977), 108-16. https://doi.org/10.1038/scientificamerican0677-108
• Lis, H., Sharon, N., Lectins as molecules and as tools. Annual Review of Biochemistry, 55 (1986), 35-67. https://doi.org/10.1146/annurev.bi.55.070186.000343
• Vierbuchen, M., Lectin Receptors. In: Seifert, G. Editors. Cell Receptors: Morphological Characterization and Pathological Aspects. Springer, Berlin, (1991), 271-361.
• Sharon, N., Lis, H., History of lectins: from hemagglutinins to biological recognition molecules. Glycobiology, 14 (11) (2004), 53r-62r. https://doi.org/10.1093/glycob/cwh122
• Brooks, S. A., Hall, D. M., Lectin histochemistry to detect altered glycosylation in cells and tissues. Methods in Molecular Biology, 878 (2012), 31-50. https://doi.org/10.1007/978-1-61779-854-2_2
• Türkmen, G., Gürel, A., Öztabak, K. Ö., Mengi, A., Ratlarda tümör gelişimi üzerine lektin'in etkisi. İstanbul Üniversitesi Veteriner Fakültesi Dergisi, 23 (2) (1997), 255-271.
• Arnusch, C. J. et al., Interference of the galactose-dependent binding of lectins by novel pentapeptide ligands. Bioorganic & Medicinal Chemistry Letters, 14 (6) (2004), 1437-40. https://doi.org/10.1016/j.bmcl.2004.01.029
• Gastman, B., Wang, K., Han, J., Zhu, Z. Y., Huang, X., Wang, G. Q., Rabinowich, H., Gorelik, E., A novel apoptotic pathway as defined by lectin cellular initiation. Biochemical and Biophysical Research Communications, 316 (1) (2004), 263-71. https://doi.org/10.1016/j.bbrc.2004.02.043
• George, S., Oh, Y., Lindblom, S., Vilain, S., Rosa, A. J., Francis, D. H., Brözel, V. S., Kaushik, R. S., Lectin binding profile of the small intestine of five-week-old pigs in response to the use of chlortetracycline as a growth promotant and under gnotobiotic conditions. Journal of Animal Science, 85 (7) (2007), 1640-50. https://doi.org/10.2527/jas.2006-662
• Köttgen, E., Reutter, W., Tauber, R., Endogene Lectine des Menschen undihre Zuckerliganden. Medizinische Klinik, 98 (12) (2003), 717-738. https://doi.org/10.1007/s00063-003-1318-1
• Vasta, G. R., Ahmed, H., Fink, N. E., Elola, M. T., Marsh, A. G., Snowden, A., Odom, E. W., Animal lectins as self/non-self recognition molecules. Biochemical and genetic approaches to understanding their biological roles and evolution. Annals of the New York Academy of Sciences, 712 (1994), 55-73. https://doi.org/10.1111/j.1749-6632.1994.tb33562.x
• Engin, A., Genel Cerrahi (Tanı ve Tedavi İlkeleri), Atlas Kitapçılık, 2000.
• Martin, F., Kearney, J. F., Marginal-zone B cells. Nature Reviews Immunology, 2 (5) (2002), 323-35. https://doi.org/10.1038/nri799
• Mehmet, K., Eşref, Y., Halis KÖ, Y., Deneysel hipertiroidizm oluşturulan tavşanlarda keratin kinaz ve kalb kası kreatin kinaz değerleleri. Turkish Journal of Biology, 22 (1) (1998), 1-5.
• Okajima, F., Ui, M., Metabolism of glucose in hyper- and hypo-thyroid rats in vivo. Glucose-turnover values and futile-cycle activities obtained with 14C- and 3H-labelled glucose. Biochemical Journal, 182 (2) (1979), 565-75. https://doi.org/10.1042/bj1820565
• Stoddart, R. W., Jones, C. J., Lectin histochemistry and cytochemistry-light microscopy : avidin-biotin amplification on resin-embedded sections. Methods in Molecular Medicine, 9 (1998), 21-39. https://doi.org/10.1385/0-89603-396-1:21
• Alonso, E., Sáez, F. J., Madrid, J. F., Hernández, F., Lectin histochemistry shows fucosylated glycoconjugates in the primordial germ cells of Xenopus embryos. Journal of Histochemistry & Cytochemistry, 51 (2) (2003), 239-43. https://doi.org/10.1177/002215540305100212
• Sauvion, N., Nardon, C., Febvay, G., Gatehouse, A. M., Rahbé, Y., Binding of the insecticidal lectin Concanavalin A in pea aphid, Acyrthosiphon pisum (Harris) and induced effects on the structure of midgut epithelial cells. Journal of Insect Physiology, 50 (12) (2004), 1137-50. https://doi.org/10.1016/j.jinsphys.2004.10.006
• Knepper, P. A., Goossens, W., Hvizd, M., Palmberg, P. F., Glycosaminoglycans of the human trabecular meshwork in primary open-angle glaucoma. Investigative Ophthalmology & Visual Science, 37 (7) (1996), 1360-7.
• Meyer, W., Godynicki, S., Tsukise, A., Lectin histochemistry of the endothelium of blood vessels in the mammalian integument, with remarks on the endothelial glycocalyx and blood vessel system nomenclature. Annals of Anatomy, 190 (3) (2008), 264-76. https://doi.org/10.1016/j.aanat.2007.11.004
• Moghaddam, F. Y., Darvish, J., Shahri, N. M., Abdulamir, A. S., Daud, S. K., Lectin Histochemistry Assay in Colon Tissues for Inter-species Characterization. American Journal of Biochemistry and Biotechnology, 5 (1) (2009), 7-13. https://doi.org/10.3844/ajbbsp.2009.7.13
• Sobral, A. P., Rego, M. J., Cavalacanti, C. L., Carvalho, L. B., Jr., Beltrão, E. I., ConA and UEA-I lectin histochemistry of parotid gland mucoepidermoid carcinoma. Journal of Oral Science, 52 (1) (2010), 49-54. https://doi.org/10.2334/josnusd.52.49
• Ofek, I., Mosek, A., Sharon, N., Mannose-specific adherence of Escherichia coli freshly excreted in the urine of patients with urinary tract infections, and of isolates subcultured from the infected urine. Infection and Immunity, 34 (3) (1981), 708-11. https://doi.org/10.1128/iai.34.3.708-711.1981
• Michaels, E. K., Chmiel, J. S., Plotkin, B. J., Schaeffer, A. J., Effect of D-mannose and D-glucose on Escherichia coli bacteriuria in rats. Urological Research, 11 (2) (1983), 97-102. https://doi.org/10.1007/bf00256954
• King, S. S., Speiser, S. A., Jones, K. L., Apgar, G. A., Wessels, S. E., Equine spermatozoal motility and fertility associated with the incorporation of d-(+)-mannose into semen extender. Theriogenology, 65 (6) (2006), 1171-9. https://doi.org/10.1016/j.theriogenology.2005.08.002
• Melo-Júnior, M., Cavalcanti, C., pontes filho, N., Carvalho, L., Beltrão, E., Carbohydrates Detection in the Hepatic Egg - Granuloma System Using Lectin Histochemistry. International Journal of Morphology, 26 (4) (2008), 967-972. https://doi.org/10.4067/S0717-95022008000400030
• Monteavaro, C. E., Soto, P., Gimeno, E. J., Echevarría, H. M., Catena, M., Portiansky, E. L., Barbeito, C. G., Histological and lectin binding changes in the genital tract of mice infected with Tritrichomonas foetus. Journal of Comparative Pathology, 138 (1) (2008), 40-5. https://doi.org/10.1016/j.jcpa.2007.08.004
• Alroy, J., Orgad, U., Ucci, A. A., Pereira, M. E., Identification of glycoprotein storage diseases by lectins: a new diagnostic method. Journal of Histochemistry & Cytochemistry, 32 (12) (1984), 1280-1284. https://doi.org/10.1177/32.12.6501863