Structure of the Asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate-linked 2-aminoethylphosphonate as a constituent of a glycoprotein

Biochemistry ◽  
1993 ◽  
Vol 32 (3) ◽  
pp. 766-775 ◽  
Author(s):  
Karl Hard ◽  
Jan M. VAn Doorn ◽  
Jane E. Thomas-Oates ◽  
Johannis P. Kamerling ◽  
Dick J. Van der Horst
1991 ◽  
Vol 196 (2) ◽  
pp. 509-517 ◽  
Author(s):  
Dick J. HORST ◽  
Jan M. DOORN ◽  
Hans VOSHOL ◽  
Michael R. KANOST ◽  
Rolf ZIEGLER ◽  
...  

Biochemistry ◽  
1995 ◽  
Vol 34 (37) ◽  
pp. 11822-11830 ◽  
Author(s):  
Vasanthy Narayanaswami ◽  
Paul M. M. Weers ◽  
Jan Bogerd ◽  
Frank P. Kooiman ◽  
Cyril M. Kay ◽  
...  

2004 ◽  
Vol 385 (11) ◽  
pp. 1113-1119 ◽  
Author(s):  
Cindy C. Pratt ◽  
Paul M.M. Weers

AbstractA new role of apolipophorin III (apoLp-III) as an immune activator has emerged recently. To gain insight into this novel function, the interaction of apoLp-III with lipopoly-saccharide (LPS) was investigated. ApoLp-III fromGalleria mellonellawas incubated with LPS fromEscherichia coliO55:B5, and analyzed by non-denaturing polyacrylamide gel electrophoresis (PAGE). Protein staining showed that apoLp-III mobility was significantly reduced. In addition, silver and LPS fluorescent staining demonstrated that LPS mobility was increased upon incubation with apoLp-III. This result suggests association of apoLp-III with LPS. Sodium dodecyl sulfate (SDS) PAGE analysis showed decreased apoLp-III mobility upon LPS addition, indicative of LPS apoLp-III interaction in the presence of SDS. The unique tyrosine residue that resides in apoLp-III was used to provide additional evidence for LPS binding interaction. In the absence of LPS, apoLp-III tyrosine fluorescence was relatively low. However, LPS addition resulted in a progressive increase in the fluorescence intensity, indicating tertiary rearrangement in the environment of tyrosine 142 upon LPS interaction. Other well-characterized apoLp-IIIs were also examined for LPS binding.Manduca sexta,Bombyx moriandLocusta migratoriaapoLp-III were all able to interact with LPS. The ability of apoLp-III to form complexes with LPS supports the proposed role of apoLp-III in innate immunity.


2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Yin Mei Phung ◽  
Johana Rodriguez ◽  
Daisy Martinon ◽  
Gezman Abdullahi ◽  
Paul M. M. Weers

Biochemistry ◽  
1994 ◽  
Vol 33 (12) ◽  
pp. 3617-3624 ◽  
Author(s):  
Paul M. M. Weers ◽  
Cyril M. Kay ◽  
Kim Oikawa ◽  
Monika Wientzek ◽  
Dick J. Van der Horst ◽  
...  

1988 ◽  
Vol 263 (8) ◽  
pp. 3960-3962
Author(s):  
H M Holden ◽  
M R Kanost ◽  
J H Law ◽  
I Rayment ◽  
M A Wells

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