TY - JOUR
T1 - The extracellular aminoterminal domain of bovine desmoglein 1 (Dsg1) is recognized only by certain pemphigous foliaceus sera, whereas its intracellular domain is recognized by both pemphigous vulgaris pemphigous foliaceus sera
AU - Dmochowski, Marian
AU - Hashimoto, Takashi
AU - Amagai, Masayuki
AU - Kudoh, Jun
AU - Shimizu, Nobuyoshi
AU - Koch, Peter J.
AU - Franke, Werner W.
AU - Nishikawa, Takeji
PY - 1994/8
Y1 - 1994/8
N2 - The major antibody binding regions of desmoglein 1 (Dsg1) in pemphigus foliaceus and pemphigus vulgaris were examined using cDNA-encoded fusion proteins combining glutathione S-transferase with various domains of bovine Dsg1, namely, the extracellular regions EC1-2, EC3-5, EC1-5, and the entire intracellular region IC. In immunoblot analyses using these fusion proteins, EC1-2, as well as EC1-5, which comprises EC1-2, were recognized by 50% of the sporadic pemphigus foliaceus sera and 45% of Brazilian pemphigus foliaceus sera that reacted with Dsg1 in immunoblotting of bovine desmosome preparations. None of these fusion proteins reacted with any sera of pemphigus vulgaris. None of these sera showed reactivity with EC3-5. In contrast, the IC domain was recognized by 91% of pemphigus vulgaris sera reactive with Dsg1 in bovine desmosome preparations, and by certain pemphigus foliaceus and Brazilian pemphigus foliaceus sera. These results indicate that major epitopes of Dsg1 recognized by pemphigus foliaceus and Brazilian pemphigus foliaceus sera are located in the extracellular ammoterminal domain EC1-2, and that sera of the Dsg1-positive pemphigus vulgaris contain antibodies against the intracellular domain, which may not play a pathogenic role. Possible reasons for this selectivity of antigen binding site are discussed.
AB - The major antibody binding regions of desmoglein 1 (Dsg1) in pemphigus foliaceus and pemphigus vulgaris were examined using cDNA-encoded fusion proteins combining glutathione S-transferase with various domains of bovine Dsg1, namely, the extracellular regions EC1-2, EC3-5, EC1-5, and the entire intracellular region IC. In immunoblot analyses using these fusion proteins, EC1-2, as well as EC1-5, which comprises EC1-2, were recognized by 50% of the sporadic pemphigus foliaceus sera and 45% of Brazilian pemphigus foliaceus sera that reacted with Dsg1 in immunoblotting of bovine desmosome preparations. None of these fusion proteins reacted with any sera of pemphigus vulgaris. None of these sera showed reactivity with EC3-5. In contrast, the IC domain was recognized by 91% of pemphigus vulgaris sera reactive with Dsg1 in bovine desmosome preparations, and by certain pemphigus foliaceus and Brazilian pemphigus foliaceus sera. These results indicate that major epitopes of Dsg1 recognized by pemphigus foliaceus and Brazilian pemphigus foliaceus sera are located in the extracellular ammoterminal domain EC1-2, and that sera of the Dsg1-positive pemphigus vulgaris contain antibodies against the intracellular domain, which may not play a pathogenic role. Possible reasons for this selectivity of antigen binding site are discussed.
KW - autoepitope
KW - fusion protein
KW - pemphigus vulgaris
KW - polymerase chain reaction
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U2 - 10.1111/1523-1747.ep12392664
DO - 10.1111/1523-1747.ep12392664
M3 - Article
C2 - 8040606
AN - SCOPUS:0028142836
SN - 0022-202X
VL - 103
SP - 173
EP - 177
JO - Journal of Investigative Dermatology
JF - Journal of Investigative Dermatology
IS - 2
ER -