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. 1974 Jul;119(1):44–49. doi: 10.1128/jb.119.1.44-49.1974

Changes in Microsporum gypseum Mycelial Wall and Spore Coat Glycoproteins During Sporulation and Spore Germination

W J Page a,1, J J Stock a
PMCID: PMC245570  PMID: 4407013

Abstract

Ethylenediamine-soluble glycoproteins were extracted from isolated Microsporum gypseum hyphal walls during sporulation and from spore coats before and after germination. This study was carried out to identify a sporulation-specific cell wall protein that possibly served as a substrate for the alkaline protease which initiated the macroconidial germination of this fungus. Analyses revealed that water-insoluble glycoprotein accounted for 10% of the ungerminated spore coat but only for 4 to 5% of the mycelial wall dry weight. This fraction was modified in its amino acid composition during sporulation, and it decreased in protein content during spore germination. Water-soluble glycoprotein, which accounted for approximately 3 to 3.5% of either the spore coat or mycelial wall dry weight, was of similar amino acid composition from both sources and did not decrease in protein content upon spore germination. The water-insoluble glycoprotein was found to be rich in leucine, aspartic acid, glycine, glutamic acid, and phenylalanine residues. The water-soluble glycoprotein was rich in proline, threonine, glycine, serine, glutamic acid, and alanine.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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