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Association of the Mycobacterial 30‐kDa Region Proteins with the Cutaneous Infiltrates of Leprosy Lesions
Author(s) -
RAMBUKKANA A.,
DAS P. K.,
KRIEG S,
FABER W. R.
Publication year - 1992
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1992.tb02938.x
Subject(s) - staining , antigen , monoclonal antibody , biology , epitope , mycobacterium leprae , immunohistochemistry , leprosy , pathology , antibody , immune system , lepromatous leprosy , immunology , microbiology and biotechnology , medicine
The granulomatous skin lesions ol human leprosy are known to be due to the cutaneous immune reaction to various mycobacterial antigens. In the present study, by immunohistochemical analysis using a previously characterized monoclonal antibody (MoAb) 3A8 we have demonstrated a selective expression of the 3A8 epitope of mycobacterial 30‐kDa proteins, the major secreted proteins of mycobacteria, in various forms of leprosy lesions across the clinical spectrum. The localization of MoAb 3A8 staining is confined to the areas of cellular infiltrates of the lesions. In tuberculoid lesions the intense 3A8 staining was seen mostly in association with the membrane of the dermal cellular infiltrates whereas in highly bacilliferous lepromatous lesions the staining seems to be diffused with granular appearance but not in the form of bacteria. In patients with reversal reaction the staining was specifically extended to cells infiltrating the epidermis. MoAb 3A8 did not show any reactivity with inflammalory skin lesions of patients other than those with leprosy. Since the 3A8 epitope of 30‐kDa proteins has been shown to be present in all cellular compartments of the mycobacteria and in the actively secreted BCG 85 antigen complex. MoAb 3A8 reactive protein(s) in leprosy lesions may be derived either from degraded somatic mycobacterial products or from antigens actively secreted by live bacilli. The latter could be true in the cases of untreated lepromatous lesions with high bacterial load since live M. leprae has also been considered to secrete corresponding 30‐kDa proteins similar to other closely related mycobacteria. By double immunoenzyme staining we clearly demonstrate the expression of 3A8 epitope on CD68 + macrophagos in the granulomas of tuberculoid leprosy, whereas in highly bacilliferous lepromatous lesions most of the double staining was seen in a diffuse pattern within the interstitial space of the cellular infiltrate as well as in the cytoplasm of CD68 + macrophages. In lesions from reversal reaction the 3A8 epitope is more strongly expressed on CD1a + dendritic Langerhans cells