@article{fdi:010049000, title = {{T}he {A}crolepiopsis assectella silk cocoon : kairomonal function and chemical characterisation}, author = {{G}authier, {N}athalie and {M}andon, {N}. and {R}enault, {S}. and {B}{\'e}n{\'e}det, {F}.}, editor = {}, language = {{ENG}}, abstract = {{T}wo soluble sericin-like polypeptides, {B}1 and {B}2, from leek moth ({A}crolepiopsis assectella) cocoons trigger host-acceptance behaviour in the parasitoid, {D}iadromus pulchellus ({P}roc. {R}oy. {S}oc. {L}ondon {B} 269 (2002) 1879). {W}e found that these polypeptides were particularly cysteine-rich and lost their ability to trigger host-acceptance behaviour after being denatured and purified. {T}his suggests that inter-disulphide bonds and the secondary structure of {B}1 and {B}2 are important for their biological activity. {W}e also isolated six insoluble polypeptides (or polypeptides of low solubility) from {A}. assectella cocoons. {A}t least four of these polypeptides triggered host-acceptance behaviour. {T}he strongest responses were observed with {P}22, a light-chain fibroin or a seroin-peptide, and {P}100, a sericin-like polypeptide that is probably more strongly associated with the silk core than are {B}1 and {B}2. {I}n conclusion, several polypeptides from different parts of the {A}. assectella silk-cocoon (the insoluble core and coating of the silk thread) are able to elicit host-acceptance behaviour in {D}. pulchellus females. {T}hese polypeptides belong to different silk protein families and are used as kairomones by this specialist parasitoid.}, keywords = {{LEPIDOPTERE} {RAVAGEUR} ; {INSECTE} ; {ENDOPARASITE} ; {PONTE} ; {RELATION} {HOTE} {PARASITE} ; {PROTEINE} ; {ACTIVITE} {BIOLOGIQUE} ; {PHYSIOLOGIE} ; {TEIGNE} {DU} {POIREAU} ; {KAIROMONE} ; {MONDE}}, booktitle = {}, journal = {{J}ournal of {I}nsect {P}hysiology}, volume = {50}, numero = {11}, pages = {1065--1074}, ISSN = {0022-1910}, year = {2004}, DOI = {10.1016/j.jinsphys.2004.09.008}, URL = {https://www.documentation.ird.fr/hor/fdi:010049000}, }