Novel surfactant proteins are involved in the structure and stability of foam nests from the frog Leptodactylus vastus

• Autor(a) principal: Hissa, Denise Cavalcante
• Data de Publicação: 2008
• Outros Autores: Vasconcelos, Ilka Maria, Carvalho, Ana Fontenele Urano, Nogueira, Vanessa Lúcia Rodrigues, Cascon, Paulo, Antunes, André Saraiva Leão Marcelo, Macedo, Gorete Ribeiro de, Melo, Vânia Maria Maciel
• Tipo de documento: Artigo
• Idioma: por
• Título da fonte: Repositório Institucional da Universidade Federal do Ceará (UFC)
• Texto Completo: http://www.repositorio.ufc.br/handle/riufc/62958
• topic: Amphibia; Leptodactylus vastus; Foam nest; Surfactants; Frog proteins

Many amphibians lay their eggs in foam nests, which allow the eggs to be deposited out of the water. Analysis of some of these foam nests has revealed that they are a rich source of proteins with unusual primary structures and remarkable surfactant activity, named ranaspumins. The aim of this work was to study the foam nests of the frog Leptodactylus vastus in order to obtain information regarding their composition and function and to improve the understanding of ranaspumins, which are probably a novel class of surfactant proteins. Analyses of the foam fluid composition showed proteins and carbohydrates that presumably are responsible for providing nutrients for the developing tadpoles. Investigation of the function of foam fluid in chemical defence revealed no significant biological activity that could be associated with recognized defence compounds. However, foam fluid presented UV absorbance, suggesting a role in protection against sun damage, which is considered to be one of the possible causes of recently reported amphibian population declines. The foam nests do not prevent the colonization of microorganisms, such as the observed bacterial community of predominantly Gram-positive bacilli. L. vastus foam fluid shows a strong surfactant activity that was associated with their proteins and this activity seems to be due mainly to a protein named Lv-ranaspumin. This protein was isolated by ion-exchange chromatography and found to be a 20kDa monomeric molecule with the following Nterminal sequence: FLEGFLVPKVVPGPTAALLKKALDD. This protein did not show any match to known proteins or structures, which suggests that it belongs to a new class of surfactant protein