A 46 kDa integral membrane protein from Mycobacterium leprae resembles a number of bacterial and mammalian membrane transport proteins

Abstract

In this paper we describe the nucleotide sequence of a 3 4 kbp region of the Mycobacterium /eprae genome. This region contains an open reading frame of 1290 bp with a coding capacity for a protein of 46179 Da, designated the 38L protein. Using antibodies against part of the 38L protein, we were able to demonstrate that the 38L protein is present in the membrane protein fraction of M. leprae. The 38L protein showed significant matches with a number of integral membrane proteins involved in the transport of small molecules through the cellular membrane. Among these are a human and a murine protein involved in melanin biosynthesis. The 38L protein might play a role in the hypopigmentation observed in leprosy patients.

Immunological and functional characterization of Mycobacterium leprae protein antigens: an overview

“…46kDa antigen. A 46kDa protein from M. leprae, designated 38L, was shown to be a cytoplasmic membrane protein (Oskam et aL, 1995). This 38L protein is likely to be involved in transport of small molecules, probably tyrosine, across the membrane.…”

The Pink‐Eyed Dilution Gene and the Molecular Pathogenesis of Tyrosinase‐Positive Albinism (OCA2)

“…Could P mutations provide protection against another prevalent disease? The Mycobacterium leprae genome encodes a 46 kDa membrane protein which shows nearly 40% homology to a region of the P protein (45,46,78). Other mycobacterial pathogens may also express this protein, which may provide the key for some form of heterozygote advantage.…”

Albinism and disease causing pathogens in Tanzania: Are alleles that are associated with OCA2 being maintained by balancing selection?

“…Although the mode(s) of leprosy transmission are not fully understood, nasal inhalation is widely accepted as the primary mode of transmission [12]. Interestingly, M. leprae has a gene, 38L, of unknown function that shares significant sequence homology to OCA2 and has been speculated to be involved in hypopigmentation [14].…”