Brugia malayi is a parasitic nematode that causes lymphatic filariasis in humans. The monoclonal antibody MF1, which mediates clearance of peripheral microfilaremia in a gerbil infection model, recognizes two stage-specific proteins, p70 and p75, in B. malayi microrflariae. cDNA coding for the MF1 antigen was sequenced, and the predicted protein sequence shows significant similarities to chitinases from bacteria and yeast. When microfilarial extracts and purified preparations of the MF1 antigen were tested for chitinase activity, strong bands of chitin-degrading activity comigrated in SDS/PAGE with p70 and p75 and showed a reductiondependent mobility shift characteristic of the MFl antigen. Thus, the MF1 antigen is microfrarial chitinase, which may function to degrade chitin-containing structures in the microfilaria or in its mosquito vector during parasite development and transmission.Lymphatic filariasis afflicts nearly 100 million people worldwide (1). Of the three species of lymphatic filariids that infect humans, Brugia malayi can most readily be maintained in the laboratory by passage between gerbils (another natural host) and a mosquito vector. Thus, B. malayi has been useful for studying pathogenesis and transmission of filariasis at the molecular level.Passive transfer of the monoclonal antibody MF1 was previously shown to mediate the transient clearance of first stage larvae, or microfilariae (mf), from the peripheral blood of gerbils infected with B. malayi (2). The MF1 antibody recognizes two stage-specific proteins (p70 and p75) in extracts of mf that appear only after the mf have matured for several days in the vertebrate host (3). The appearance of the MF1 antigen corresponds with the onset of the parasite's ability to infect the mosquito (3).It was thus of great interest to define more precisely the role of the MF1 antigen in filarial development and transmission. With the expectation that the proteins' sequences might clarify their function, we obtained partial amino acid sequences for p70 and p75 and then used this information to isolate and to sequence the corresponding cDNA.1 We report here that the predicted protein sequence of the MF1 antigen has several regions of significant similarity to bacterial and yeast chitinases. Furthermore, the native MF1 antigen is demonstrated to degrade chitin in vitro.MATERIALS AND METHODS Parasite Material. Gerbils (Meriones unguiculatus) were infected intraperitoneally with B. malayi either in our own facilities or at the Filariasis Repository Research Service, Athens, GA. mf were purified and proteins were extracted as described (3). Poly(A) mRNA was isolated from purified mf according to Cox and Smulian (4). Genomic DNA was made from adult B. malayi as described (5).Protein Purification and Amino Acid Sequencing. The MF1 antigen was partially purified from extracts of mf by DE-52 chromatography as described (6). N-terminal sequence analysis was performed on the combined p70 and p75 following elution with 0.5 M NaCI from DE-52, using an ABI model 4...