Skip to main content
SpringerLink
Log in

Potential for Penetration of Passive Barriers to Fungal Invasion in Humans

  • Chapter
The Fungal Spore and Disease Initiation in Plants and Animals

Abstract

The principal passive barriers to fungal invasion in humans are epithelial surfaces. For any fungal propagule that has successfully reached and attached itself to epithelia, penetration of the epithelial surface is the necessary next stage of the pathological process. The extent to which a fungus can penetrate epithelia solely by exerting mechanical pressure on the host cells is unknown: it seems likely that most, if not all, instances of fungal penetration involve enzymatic degradation of host surface macromolecules. The focus of this chapter will therefore be on the elaboration by fungi of enzymes that aid in the penetration of the host’s passive barriers.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 249.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Barlow, A. J. E., and Chattaway, F. W., 1955, Attack of chemically modified keratin by certain dermatophytes, J. Invest. Dermatol. 24: 65–74.

    PubMed  CAS  Google Scholar 

  • Barrett-Bee, K., Hayes, Y., Wilson, R. G., and Ryley, J. F.,1985, A comparison of phospholipase activity, cellular adherence and pathogenicity of yeasts, J. Gen. Microbial. 131: 1217–1221.

    Google Scholar 

  • Borg, M., and Rüchel, R., 1988, Expression of extracellular acid proteinase by proteolytic Candida spp. during experimental infection of oral mucosa, Infect. Immun. 56: 626–631.

    PubMed  CAS  Google Scholar 

  • Bradbury, J. H., 1973, The structure and chemistry of keratin fibers, Adv. Protein Chem. 27: 111–211.

    Article  PubMed  CAS  Google Scholar 

  • Chattaway, F W, Ellis, D. A., and Barlow, A. J. E., 1963, Peptidases of dermatophytes, J. Invest. Dermatol. 41: 31–37.

    PubMed  CAS  Google Scholar 

  • Chesters, C. G. C., and Mathison, G. E., 1963, The decomposition of wool keratin by Keratinomyces ajelloi, Sabouraudia 2: 225–237.

    Article  Google Scholar 

  • Cohen, B. L., 1977, The proteases of aspergilli, in: Genetics and Physiology of Aspergillus ( J. E. Smith and J. A. Pateman, eds.), Academic Press, New York, pp. 281–292.

    Google Scholar 

  • Collins, J. P., Grappel, S. F, and Blank, F., 1973, Role of keratinases in dermatophytosis. II. Fluorescent antibody studies with keratinase II of Trichophyton mentagrophytes, Dermatologica 146: 95–100.

    Article  PubMed  CAS  Google Scholar 

  • Cruickshank, C. N. D., and Trotter, M. D., 1956, Separation of epidermis from dermis by filtrates of Richophyton mentagrophytes, Nature 177: 1085–1086.

    Article  PubMed  CAS  Google Scholar 

  • Daniels, G., 1953, The digestion of human hair by Microsporum canis Bodin, J. Gen. Microbiol. 8: 289–294.

    Article  PubMed  CAS  Google Scholar 

  • Das, S. K., and Banerjee, A. B., 1978, Lipolytic enzymes of Trichophyton rubrum, Sabouraudia 15: 313–323.

    Article  Google Scholar 

  • Das, S. K., and Banerjee, A. B., 1982, Effect of undecanoic acid on the products of exocellular lipolytic and keratinolytic enzymes by undecanoic acid-sensitive and -resistant strains of Pichophyton rubrum, Sabouraudia 20: 179–184.

    Article  PubMed  CAS  Google Scholar 

  • Day, W C., Toncic, P, Stratman, S. L., Leeman, U., and Harmon, S. R., 1968, Isolation and properties of an extracellular protease of Trichophyton granulosum, Biochim. Biophys. Acta 167: 597–606.

    Article  PubMed  CAS  Google Scholar 

  • Deshmukh, S. K., and Agrawal, S. C., 1982, In vitro degradation of human hair by some keratinophilic fungi, Mykosen 25: 45458.

    Google Scholar 

  • Deshmukh, S. K., and Agrawal, S. C., 1985, Degradation of human hair by some dermatophytes and other keratinophilic fungi, Mykosen 28: 463–466.

    Article  PubMed  CAS  Google Scholar 

  • Eleuterio, M. K., Grappel, S. F, Caustic, C. A., and Blank F, 1973, Role of keratinases in dermatophytosis. III. Demonstration of delayed hypersensitivity to keratinases by the capillary tube migration test, Dermatologica 147: 255–260.

    Article  PubMed  CAS  Google Scholar 

  • Evolceanu, R., and Lazar, M., 1960, Le Problème de l’existence et de la mise en évidence des ferments kératinolytique chez les dermatophytes, Mycopathol. Mycol. Appl. 12: 216–222.

    Article  CAS  Google Scholar 

  • Gabriel, B. P, 1968, Histochemical study of the insect cuticle infected by the fungus Entomophthora coronata, J. Invertebr. Pathol. 11: 82–89.

    Article  Google Scholar 

  • Grappel, S. F, and Blank, F., 1972, Role of keratinase in dermatophytosis. I. Immune responses of guinea-pigs: infected with Trichophyton mentagrophytes and guinea-pigs immunized with keratinases, Dermatologica 145: 245–255.

    Article  PubMed  CAS  Google Scholar 

  • Guentzel, M. N., Cole, G. T., and Pope, L. M., 1985, Animal models for candidiasis, in: Current Topics in Medical Mycology, Volume 1 ( M. R. McGinnis, ed.), Springer-Verlag, Berlin, pp. 57–115.

    Chapter  Google Scholar 

  • Hattori, M., Yoshiura, K., Negi, M., and Ogawa, H., 1984, Keratinolytic proteinase produced by Candida albicans, Sabouraudia J. Med. Vet. Mycol. 22: 175–183.

    Article  CAS  Google Scholar 

  • Hose, H., 1976, Decomposition of native keratin by dermatophyte fungi, Ph.D. thesis, Department of Microbiology, University of Leeds, Leeds, U.K.

    Google Scholar 

  • Kennedy, M. J., 1988, Adhesion and association mechanisms of Candida albicans, in: Current Topics in Medical Mycology, Volume 2 ( M. R. McGinnis, ed.), Springer-Verlag, Berlin, pp. 73–169.

    Chapter  Google Scholar 

  • Kennedy, M., Volz, P A., Edwards, C. A., and Yancey, R. J., 1987, Mechanisms of association of Candida albicans with intestinal mucosa, J. Med. Microbial. 24: 333–342.

    Article  CAS  Google Scholar 

  • Kothary, M. H., Chase, T., Jr., and MacMillan, J. D., 1984, Correlation of elastase production by some strains of Aspergillus fumigants with ability to cause pulmonary invasive aspergillosis in mice, Infect. Immun. 43: 320–327.

    PubMed  CAS  Google Scholar 

  • Krause, W, Matheis, H., and Wulf, K., 1969, Fungaemia and funguria after oral administration of Candida albicans, Lancet 1: 598–599.

    Article  PubMed  CAS  Google Scholar 

  • Kunert, J., 1972a, The digestion of human hair by the dermatophyte Microsporum gypseum in a submerged culture, Mykosen 15: 59–71.

    Article  PubMed  CAS  Google Scholar 

  • Kunert, J., 1972b, Thiosulphate esters in keratin attacked by dermatophytes, Sabouraudia 10: 6–13.

    Article  PubMed  CAS  Google Scholar 

  • Kunert, J., 1975, Formation of sulphate, sulphite and S-sulphocysteine by the fungus Microsporum gypseum during growth on cystine, Folia Microbial. 20: 142–151.

    Article  CAS  Google Scholar 

  • Kwon-Chung, K. J., Lehman, D., Good, C., and Magee, P T., 1985, Genetic evidence for role of extracellular proteinase in virulence of Candida albicans, 49: 571–575.

    CAS  Google Scholar 

  • Lee, K. H., Park K. K., Park, S. K., and Lee, J. B., 1987, Isolation, purification and characterization of keratinolytic proteinase from Microsporum canis, Yonsei Med. J. 28: 131–138.

    PubMed  CAS  Google Scholar 

  • Lupan, D. M., and Nziramasanga, P, 1985, Elastase activity of fungi with anamorphs similar to Coccidioides immitis, Mycopathologia 92: 169–171.

    Article  PubMed  CAS  Google Scholar 

  • Lupan, D. M., and Nziramasanga, P., 1986, Collagenolytic activity of Coccidioides immitis, Infect. Immun. 51: 360–361.

    PubMed  CAS  Google Scholar 

  • Macdonald, F, and Odds, E. C., 1983, Virulence for mice of a proteinase-secreting strain of Candida albicans and a proteinase-deficient mutant, J. Gen. Microbial. 129: 431–438.

    CAS  Google Scholar 

  • Macfadyen, A., 1896, A contribution to the biology of the ringworm organism, J. Pathol. Bacterial. 3: 176–183.

    Article  Google Scholar 

  • McQuade, A. B., 1964, Microbiological degradation of wool, Dermatologica 128: 249–266.

    Article  PubMed  CAS  Google Scholar 

  • Mandels, G. R., Stahl, W. H., and Levinson, H. S., 1948, Structural changes in wool degraded by the ringworm fungus Microsporum gypseum and other organisms, Text. Res. J. 18: 224–231.

    Article  CAS  Google Scholar 

  • Meevootisom, V., and Niederpruem, D. J., 1979, Control of exocellular proteases in dermatophytes and especially Trichophyton rubrum, Sabouraudia 17: 91–106.

    Article  PubMed  CAS  Google Scholar 

  • Mikx, E. H., and DeJong, M. H., 1987, Keratinolytic activity of cutaneous and oral bacteria, Infect. Immun. 55: 621–625.

    PubMed  CAS  Google Scholar 

  • Miyaji, M., and Nishimura, K., 1977, Relationship between proteolytic activity of Aspergillus fumigatus and the fungal invasiveness of mouse brain, Mycopathologia 62: 161–166.

    Article  PubMed  CAS  Google Scholar 

  • Negi, M., Tsuboi, R., Matsui, T., and Ogawa, H., 1984, Isolation and characterization of proteinase from Candida albicans, J. Invest. Dermatol. 83: 32–36.

    Article  PubMed  CAS  Google Scholar 

  • Nobre, G., and Viegas, M. P., 1972, Lipolytic activity of dermatophytes, Mycopathol. Mycol. Appl. 46: 319–323.

    Article  PubMed  CAS  Google Scholar 

  • Novai, J. J., and Nickerson, W. J., 1959, Decomposition of native keratin by Streptomyces fradiae, J. Bacteriol. 77:251–263.

    Google Scholar 

  • Odds, E. C., 1985, Candida albicans proteinase as a virulence factor in the pathogenesis of Candida infections, Zentralbl. Bakteriol. Hyg. [A] 260: 539–542.

    CAS  Google Scholar 

  • Odds, E. C., 1988, Candida and Candidosis, 2nd ed., Baillière Tindall, London.

    Google Scholar 

  • O’Sullivan, J., and Mathison, G. E., 1971, The localization and secretion of a proteolytic enzyme complex by the dermatophytic fungus Microsporum canis, J. Gen. Microbial. 68: 319–326.

    Article  Google Scholar 

  • Price, M. F., and Cawson, R. A., 1977, Phospholipase activity in Candida albicans, Sabouraudia 15: 179–185.

    Article  PubMed  CAS  Google Scholar 

  • Pugh, D., and Cawson, R. A., 1975, The cytochemical localization of phospholipase a and lysophospholipase in Candida albicans, Sabouraudia 13: 110–115.

    Article  PubMed  Google Scholar 

  • Ragot, J., 1966, Activité kératinolytique du Keratinomyces ajelloi vanbr. sur la laine non dénaturée, C. R. Acad. Sci. Ser. D 262: 412–415.

    CAS  Google Scholar 

  • Ragot, J., 1967, Activité protéolytique du Keratinomyces ajelloi vanbr. en présence de kératine, C. R. Acad. Sci. Ser. D 265: 493–496.

    CAS  Google Scholar 

  • Ragot, J., 1969, Influence de certains agents de sterilisation sur la kératine, Mycopathol. Mycol. Appl. 39: 177–186.

    Article  CAS  Google Scholar 

  • Raubitschek, E, 1961, Mechanical versus chemical keratinolysis by certain dermatophytes, Sabouraudia 1: 87–90.

    Article  PubMed  CAS  Google Scholar 

  • Ray, T. L., and Payne, C. D., 1988, Scanning electron microscopy of epidermal adherence and cavitation in murine candidiasis: A role for Candida acid proteinase, Infect. Immun. 56: 1942–1949.

    PubMed  CAS  Google Scholar 

  • Rippon, J. W, 1967, Elastase: Production by ringworm fungi, Science 157: 947.

    Article  PubMed  CAS  Google Scholar 

  • Rippon, J. W, 1968, Extracellular collagenase from Trichophyton schoenleinii, J. Bacteriol. 95: 43–46.

    PubMed  CAS  Google Scholar 

  • Rippon, J. W, 1988, Medical Mycology, 3rd ed., Saunders, Philadelphia, p. 158.

    Google Scholar 

  • Rippon, J. W, and Varadi, D. P., 1968, The elastases of pathogenic fungi and actinomycetes, J. Invest. Dermatol. 50: 54–58.

    PubMed  CAS  Google Scholar 

  • Roberts, E. F., and Doetsch, R. N., 1967, Purification of a highly active protease from a Microsporum species, Antonie van Leeuwenhoek J. Microbial. Serol. 33: 145–152.

    Article  CAS  Google Scholar 

  • Rogozhkina, N. M., Klimova, I. M., and Zelenskaya, L. I., 1977, Izuchenia nekotorykh uslovii abrazovaniya proteazy Coccidioides immitis, Zh. Mikrobiol. Epidemiol. Immunobiol. 8: 87–90.

    PubMed  Google Scholar 

  • Ruffin, P., Andrieu, S., Biserte, G., and Signet, J., 1976, Sulphitolysis in keratinolysis. Biochemical proof, Sabouraudia 14: 181–184.

    Article  PubMed  CAS  Google Scholar 

  • Sanyal, A. K., Das, S. K., and Banerjee, A. B., 1985, Purification and partial characterization of an exocellular proteinase from Trichophyton rubrum, Sabouraudia 23: 165–178.

    Article  PubMed  CAS  Google Scholar 

  • Skofepovâ, M., and Hauck, H.,1987, Extracellular proteinases of Trichophyton rubrum and the clinical picture of tinea, Mykosen 30: 25–27.

    Google Scholar 

  • Stahl, W. H., McQue, B., Mandels, G. R., and Siu, R. G. H., 1949, Studies on the microbiological degradation of wool. I. Sulfur metabolism, Arch. Biochem. 20: 422–432.

    PubMed  CAS  Google Scholar 

  • Stahl, W. H., McQue, B., Mandels, G. R., and Siu, R. G. H., 1950a, Studies on the microbiological degradation of wool. Digestion of normal and modified fibrillar proteins, Text. Res. J. 20: 570–579.

    Article  CAS  Google Scholar 

  • Stahl, W. H., McQue, B., and Siu, R. G. H., 1950b, Studies on the microbiological degradation of wool. II. Nitrogen metabolism, Arch. Biochem. 27: 211–220.

    PubMed  CAS  Google Scholar 

  • Staib, F., 1985, Pleural fluid as nutrient substratum for Aspergillus fumigatus and A. jlavus. Submerged growth in pleural fluid and extracellular proteolysis in pleural fluid agar, Zentralbl. Bakteriol. Mikrobiol. Hyg. [A] 260: 566–571.

    CAS  Google Scholar 

  • Takiuchi, I., Higuchi, D., and Negi, M., 1981, The effect of keratinase on human epidermis, especially on stratum corneum, Jpn. J. Dermatol. 91: 119–125.

    CAS  Google Scholar 

  • Tltkiuchi, I., Higuchi, D., Sei, Y., and Koga, M., 1982, Isolation of an extracellular proteinase (keratinase) from Microsporum canis, Sabouraudia 20: 281–288.

    Article  Google Scholar 

  • Thkiuchi, I., Higuchi, D., Sei, Y., and Koga, M., 1983, Immunological studies of an extracellular keratinase, J. Dermatol. (Tokyo) 10: 327–330.

    Google Scholar 

  • Takiuchi, I., Sei, Y., Takagi, H., and Negi, M., 1984, Partial characterization of the extracellular keratinase from Microsporum canis, Sabouraudia 22: 219–224.

    Article  PubMed  CAS  Google Scholar 

  • Volkheimer, G., Schulz, E. H., Aurich, I., Strauch, S., Beuthin, K., and Wendlandt, H., 1968, Persorption of particles, Digestion 1: 78–80.

    Article  PubMed  CAS  Google Scholar 

  • Wawrzkicwicz, K., Lobarzewski, J., and Wolski, T., 1987, Intracellular keratinase of Trichophyton gallinae, J. Med. Vet. Mycol. 25: 261–268.

    Article  Google Scholar 

  • Weary, P. E., and Canby, C. M., 1967, Keratinolytic activity of Trichophyton schoenleinii, Trichophyton rubrum and Trichophyton mentagrophytes, J. Invest. Dermatol. 42: 240–248.

    Google Scholar 

  • Weary, P. E., and Canby, C. M., 1969, Further observations on the keratinolytic activity of Trichophyton schoenleinii and Trichophyton rubrum, J. Invest. Dermatol. 53 58–63.

    PubMed  CAS  Google Scholar 

  • Weary, P. E., Canby, C. M., and Cowley, E. P., 1965, Keratinolytic activity of Microsporum c. anis and Microsporum gypseum, J. Invest. Dermatol. 44: 300–310.

    PubMed  CAS  Google Scholar 

  • Yu, R. J., Harmon, S. R., and Blank, F, 1968, Isolation and purification of an extracellular keratinase of Trichophyton mentagrophytes, J. Bacteriol. 96: 1435–1436.

    PubMed  CAS  Google Scholar 

  • Yu, R. J., Harmon, S. R., and Blank, E, 1969a, Hair digestion by a keratinase of Trichophyton mentagrophytes, J. Invest. Dermatol. 53: 166–171.

    PubMed  CAS  Google Scholar 

  • Yu, R. J., Harmon, S. R., Wachter, P. E., and Blank, F., 1969b, Amino acid composition and specificity of a keratinase of Trichophyton mentagrophytes, Arch. Biochem. Biophys. 135: 363–370.

    Article  PubMed  CAS  Google Scholar 

  • Yu, R. J., Harmon, S. R., Grappel, S. F., and Blank, F., 1971, Two cell-bound keratinases of Trichophyton mentagrophytes, J. Invest. Dermatol. 56: 27–32.

    Article  PubMed  CAS  Google Scholar 

  • Yuan, L., and Cole, G. T., 1987, Isolation and characterization of an extracellular proteinase of Coccidioides immitis, Infect. Immun. 55: 1970–1978.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Bacteriology and Mycology, Janssen Research Foundation, B-2340, Beerse, Belgium

    Frank C. Odds

Authors
  1. Frank C. Odds
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. The University of Texas at Austin, Austin, Texas, USA

    Garry T. Cole

  2. New York State Agricultural Experiment Station, Cornell University, Geneva, New York, USA

    Harvey C. Hoch

Rights and permissions

Reprints and permissions

Copyright information

© 1991 Springer Science+Business Media New York

About this chapter

Cite this chapter

Odds, F.C. (1991). Potential for Penetration of Passive Barriers to Fungal Invasion in Humans. In: Cole, G.T., Hoch, H.C. (eds) The Fungal Spore and Disease Initiation in Plants and Animals. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2635-7_13

Download citation

  • DOI: https://doi.org/10.1007/978-1-4899-2635-7_13

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4899-2637-1

  • Online ISBN: 978-1-4899-2635-7

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation