Studies on localization and protein ligands of \emph {Galleria mellonella} apolipophorin III during immune response against different pathogens
PBN-AR
Instytucja
Wydział Inżynierii Materiałowej i Ceramiki (Akademia Górniczo-Hutnicza im. Stanisława Staszica w Krakowie)
Informacje podstawowe
Główny język publikacji
EN
Czasopismo
Journal of Insect Physiology (35pkt w roku publikacji)
ISSN
0022-1910
EISSN
1879-1611
Wydawca
London; New York : Pergamon Press
DOI
Rok publikacji
2018
Numer zeszytu
Strony od-do
18--27
Numer tomu
105
Link do pełnego tekstu
Identyfikator DOI
Liczba arkuszy
0.71
Autorzy
(liczba autorów: 11)
Pozostali autorzy
+ 10
Słowa kluczowe
EN
apolipophorin III
Galleria mellonella
apolipophorin II
hexamerin
arylphorin
apolipophorin I
Streszczenia
Język
EN
Treść
A lipid-binding protein apolipophorin III (apoLp-III), an exchangeable component of lipophorin particles, is involved in lipid transport and immune response in insects. In Galleria mellonella, apoLp-III binding to high-density lipophorins and formation of low-density lipophorin complexes upon immune challenge was reported. However, an unanswered question remains whether apoLp-III could form different complexes in a pathogen-dependent manner. Here we report on pathogen- and time-dependent alterations in the level of apoLp-III free and lipophorin-bound form that occur in the hemolymph and hemocytes shortly after immunization of G. mellonella larvae with different pathogens, i.e. Gram-negative bacterium Escherichia coli, Gram-positive bacterium Micrococcus luteus, yeast-like fungus Candida albicans, and filamentous fungus Fusarium oxysporum. These changes were accompanied by differently persistent re-localization of apoLp-III in the hemocytes. The apoLp-III-interacting proteins were recovered from immune hemolymph by affinity chromatography on a Sepharose bed with immobilized anti-apoLp-III antibodies. ApoLp-I, apoLp-II, hexamerin, and arylphorin were identified as main components that bound to apoLp-III; the N-terminal amino acid sequences of G. mellonella apoLp-I and apoLp-II were determined for the first time. In the recovered complexes, the pathogen-dependent differences in the content of individual apolipophorins were detected. Apolipophorins may thus be postulated as signaling molecules responding in an immunogen-dependent manner in early steps of G. mellonella immune response.
Cechy publikacji
original article
peer-reviewed
Inne
System-identifier
idp:111729
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