Abstract
Sporothrix schenckii produces two extracellular proteinases, namely proteinase I and II. Proteinase I is a serine proteinase, inhibited by chymostatin, while proteinase II is an aspartic proteinase, inhibited by pepstatin. Studies on substrate specificity and the effect of proteinase inhibitors on cell growth suggest an important role for these proteinases in terms of fungal invasion and growth. There has, however, been no evidence presented demonstrating thatS. schenckii produces 2 extracellular proteinases in vivo. In order to substantiate the in vivo production of proteinases and to attempt a preliminary serodiagnosis of sporotrichosis, serum antibodies against 2 proteinases were assayed usingS. schenckii inoculated hairless mice. Subsequent to an intracutaneous injection ofS. schenckii to the mouse skin, nodules spontaneously formed and disappeared for a period of 4 weeks. Histopathological examination results were in accordance with the microscopic observations. Micro-organisms disappeared during the fourth week. Serum antibody titers against purified proteinases I and II were measured weekly, using enzyme-linked immunosorbent assay (EIA). As a result, the time course of the antibody titers to both proteinases I and II were parallel to that of macroscopic and microscopic observations in an experimental mouse sporotrichosis model. These results suggest thatS. schenckii produces both proteinases I and II in vivo. Moreover, the detection of antibodies against these proteinases can contribute to a serodiagnosis of sporotrichosis.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
References
Karlin JV, Nielsen HS Jr. Serologic aspects of sporotrichosis. J Infect Dis 1970; 121: 316–27.
Norden A. Sporotrichosis: Clinical and laboratory features and a serologic study in experimental animals and humans. Acta Path Microbiol Scand 1951; 89s: 1–119.
de Albornoz MB, Villanueva E, de Tortes ED. Application of immunoprecipitation techniques to the diagnosis of cutaneous and extracutaneous forms of sporotrichosis. Mycopathologica 1984; 85: 177–83.
Scott SM, Peasley ED, Crymes TP. Pulmonary sporotrichosis. Report of two cases with cavitation. N Eng J Med 1961; 265: 453–57.
Post GW, Jackson A, Garber PE, Veach GF. Pulmonary sporotrichosis. Dis Chest 1958; 34: 455–59.
Welsh RD, Dolan CT. Sporothrix whole yeast agglutination test: Low-titer reactions of sera of subjects not known to have sporotrichosis. Am J Clin Pathol 1973; 59: 82–5.
Scott EN, Kaufman L, Brown AC, Muchmore HG. Serologic studies in the diagnosis and management of meningitis due toSporothrix schenckii. N Eng J Med 1987; 317: 935–40.
Scott EN, Muchmore HG, Parkinson AJ. Enzyme and radioimmunoassays in human sporotrichosis. In: Proceedings of the 8th Congress of the International Society for Human Animal Mycology, Massey University, Palmerston North, New Zealand, 1982: 212–15.
Lloyd K, Bitoon MA. Isolation and Purification of a peptidorhamnomannan from the yeast form ofSporothrix schenckii: Structural and immunochemical studies. J Immunol 1971; 107: 663–71.
Tsuboi R, Ko I-J, Takamori K, Ogawa H. Isolation of a keratinolytic proteinase fromTrichophyton mentagrophytes with enzymatic activity at acidic pH. Infect Immun 1989; 57: 3479–83.
Hattori M, Yoshiura K, Negi M, Ogawa H. Keratinolytic proteinase produced byCandida albicans. Sabouraudia 1984; 22: 175–83.
Negi M, Tsuboi R, Matsui T, Ogawa H. Isolation and characterization of proteinase fromCandida albicans: Substrate specificity. J Invest Dermatol 1984; 83: 32–6.
Tsuboi R, Kurita Y, Iwahara K, Hirotani T, Matsuda K, Negi M, Ogawa H. The biological role of keratinolytic proteinase (KPase) and its inhibitor on the growth ofCandida albicans. In: Ogawa H, Lazarus GS, Hopsu-Havu, eds. The biological role of proteinases and their inhibitors in skin. Tokyo: University of Tokyo Press, 1985; 161–73.
Tsuboi R, Kurita Y, Negi M, Ogawa H. A specific inhibitor of keratinolytic proteinase fromCandida albicans could inhibit the cell growth ofC. albicans. J Invest Dermatol 1985; 85: 438–40.
Tsuboi R, Matsuda K, Ko I-J, Ogawa H. Correlation between culture medium pH, extracellular proteinase activity, and cell growth ofCandida albicans in insoluble stratum corneum-supplemented media. Arch Dermatol Res 1989; 281: 342–45.
Tsuboi R, Sanada T, Takamori K, Ogawa H. Isolation and properties of extracellular proteinases fromSporothrix schenckii. J Bacteriol 1987; 169: 4104–9.
Tsuboi R, Sanada T, Ogawa H. Influence of culture medium pH and proteinase inhibitors on extracellular proteinase activity and cell growth ofSporothrix schenckii. J Clin Microbiol 1988; 26: 1431–33.
Rojanavanich V, Yoshiike T, Tsuboi R, Takamori K, Ogawa H. Purification and characterization of an extracellular proteinase fromHendersonula toruloidea. Infect Immun 1990; 58: 2856–61.
Rippon JW. Sporotrichosis. In: Medical mycology: The pathogenic fungi and the pathogenic actinomycetes. Philadelphia: WB Saunders, 1988: 325–52.
Feldmann M, Male D. Cell cooperation in the immune response. In: Roitt IM, Brostoff J, Male DK, eds. London: Churchill Livingstone, 1990: 1–12.
Lefvert AK, Link H. IgG production within the central nervous system: A critical review of proposed formulae. Ann Neurol 1985; 17: 13–20.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Yoshiike, T., Lei, PC., Komatsuzaki, H. et al. Antibody raised against extracellular proteinases ofSporothrix schenckii inS. schenkii inoculated hairless mice. Mycopathologia 123, 69–73 (1993). https://doi.org/10.1007/BF01365082
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF01365082