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In this study, we describe the cloning, expression, functional evaluation, and potential biotechnological application of cDNAs, which code for two new phospholipase D isoforms, LIPLD1 and LIPLD2, of the spider <jats:italic>Loxosceles laeta<\/jats:italic>. The recombinant protein rLIPLD1 had hydrolytic activity on sphingomyelin and in vitro hemolytic activity on human red blood cells, whereas rLIPLD2 was inactive. The purified recombinant proteins and the venom are recognized by polyclonal anti\u2010rLIPLD1 and rLIPLD2 sera produced in animals and conferred immunoprotection against the venom. These new isoforms reinforce the importance of the multigene family of phospholipases\u2010D present in <jats:italic>Loxosceles<\/jats:italic> spiders. A highly immunogenic inactive isoform such as rLIPLD2 raises important expectation for its use as a potential immunogenic inducer of the immunoprotective response to the toxic action of the venom of <jats:italic>Loxosceles laeta<\/jats:italic>. \u00a9 2011 Wiley Periodicals, Inc. J Biochem Mol Toxicol 25:393\u2013403 2011; View this article online at <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"wileyonlinelibrary.com\">wileyonlinelibrary.com<\/jats:ext-link>. 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