Binding Characteristics of Bovine Lactoferrin to the Cell Surface ofClostridiumSpecies and Identification of the Lactoferrin-binding Protein

1998 ◽  
Vol 62 (8) ◽  
pp. 1476-1482 ◽  
Author(s):  
Shinichi TOMITA ◽  
Nami SHIRASAKI ◽  
Hideshi HAYASHIZAKI ◽  
Jun MATSUYAMA ◽  
Yoshimi BENNO ◽  
...  
Keyword(s):  
Cell Surface ◽  
Binding Protein ◽  
Bovine Lactoferrin ◽  
Binding Characteristics

Foetal steroid binding protein in British and Japanese women

1987 ◽  
Vol 114 (4) ◽  
pp. 584-588 ◽  
Author(s):  
M. Jawed Iqbal ◽  
Alastair Forbes ◽  
Mark L. Wilkinson ◽  
John W. Moore ◽  
Roger Williams ◽  
...  
Keyword(s):  
Ovarian Function ◽  
Binding Protein ◽  
Premenopausal Women ◽  
Japanese Women ◽  
Sex Hormone Binding Globulin ◽  
Partial Purification ◽  
Enzyme Linked Immunosorbent Assay ◽  
Binding Characteristics ◽  
Steroid Binding ◽  
Steroid Binding Protein

Abstract. In order to examine the newly-discovered sex-steroid binding protein, foetal steroid binding protein (FSBP) in different populations, its binding characteristics and its level were studied by two-tier column ligand binding assay and enzyme-linked immunosorbent assay (ELISA) respectively. In 10 Japanese premenopausal women, analysis of 5α-dihydrotestosterone (DHT) binding in the Cibacron Blue 3GA-Sepharose 6B portion of the column showed a rising plateau pattern with a mean maximum binding of 31.1 ± 7.41%, whereas of 9 similar British women, 8 displayed unsaturable, non-cooperative binding of 11.6 ± 8.22% (P < 0.01). After partial purification of FSBP in these samples, the protein exhibited saturable binding kinetics, median binding 25 (interquartiles 23–34) and 19 (13–25) nmol DHT/l in Japanese and British women, respectively (P < 0.05). By analyzing FSBP by ELISA in 56 Japanese (45 premenopausal) and 59 British (25 premenopausal) women, higher levels were obtained in the whole Japanese group (P = 0.0016) and in the premenopausal Japanese women (P = 0.018) than in their British counterparts. In both nationalities, FSBP levels were higher in premenopausal women, and there was a significant negative correlation of FSBP with age in both populations, particularly in postmenopausal women. FSBP levels did not correlate with weight, parity, sex hormone binding globulin or albumin levels. The influence of FSBP on free steroid levels remains unclear, but some relationship with ovarian function seems a possibility.

scholarly journals Identification of a novel cell attachment domain in the HIV-1 Tat protein and its 90-kDa cell surface binding protein.

1993 ◽  
Vol 268 (7) ◽  
pp. 5279-5284
Author(s):  
B.S. Weeks ◽  
K. Desai ◽  
P.M. Loewenstein ◽  
M.E. Klotman ◽  
P.E. Klotman ◽  
...  
Keyword(s):  
Cell Surface ◽  
Cell Attachment ◽  
Binding Protein ◽  
Tat Protein ◽  
Surface Binding ◽  
Cell Surface Binding ◽  
Hiv 1

Molecular and Functional Characterization of One Odorant-Binding Protein Gene OBP3 in Bemisia tabaci (Hemiptera: Aleyrodidae)

2019 ◽  
Author(s):  
Ran Wang ◽  
Yuan Hu ◽  
Peiling Wei ◽  
Cheng Qu ◽  
Chen Luo
Keyword(s):  
Host Plant ◽  
Bemisia Tabaci ◽  
Binding Protein ◽  
Insect Pest ◽  
Critical Role ◽  
Functional Characterization ◽  
Odorant Binding Protein ◽  
Binding Characteristics ◽  
And Function ◽  
Odorant Binding

Abstract Odorant binding proteins (OBPs) of insects play a critical role in chemical perceptions and choice of insect host plant. Bemisia tabaci is a notorious insect pest which can damage more than 600 plant species. In order to explore functions of OBPs in B. tabaci, here we investigated binding characteristics and function of odorant-binding protein 3 in B. tabaci (BtabOBP3). The results indicated that BtabOBP3 shows highly similar sequence with OBPs of other insects, including the typical signature motif of six cysteines. The recombinant BtabOBP3 protein was obtained, and the evaluation of binding affinities to tested volatiles of host plant was conducted, then the results indicated that β-ionone had significantly higher binding to BtabOBP3 among other tested plant volatiles. Furthermore, silencing of BtabOBP3 significantly altered choice behavior of B. tabaci to β-ionone. In conclusion, it has been demonstrated that BtabOBP3 exerts function as one carrier of β-ionone and the results could be contributed to reveal the mechanisms of choosing host plant in B. tabaci.

scholarly journals The VP5 Domain of VP4 Can Mediate Attachment of Rotaviruses to Cells

2000 ◽  
Vol 74 (2) ◽  
pp. 593-599 ◽  
Author(s):  
Selene Zárate ◽  
Rafaela Espinosa ◽  
Pedro Romero ◽  
Ernesto Méndez ◽  
Carlos F. Arias ◽  
...  
Keyword(s):  
Cell Surface ◽  
Binding Assay ◽  
Cell Attachment ◽  
Wild Type ◽  
Binding Assays ◽  
Virus Binding ◽  
Binding Characteristics ◽  
Surface Receptors ◽  
Infectivity Assay ◽  
Fusion Products

ABSTRACT Some animal rotaviruses require the presence of sialic acid (SA) on the cell surface to infect the cell. We have isolated variants of rhesus rotavirus (RRV) whose infectivity no longer depends on SA. Both the SA-dependent and -independent interactions of these viruses with the cell are mediated by the virus spike protein VP4, which is cleaved by trypsin into two domains, VP5 and VP8. In this work we have compared the binding characteristics of wild-type RRV and its variant nar3 to MA104 cells. In a direct nonradioactive binding assay, both viruses bound to the cells in a saturable and specific manner. When neutralizing monoclonal antibodies directed to both the VP8 and VP5 domains of VP4 were used to block virus binding, antibodies to VP8 blocked the cell attachment of wild-type RRV but not that of the variant nar3. Conversely, an antibody to VP5 inhibited the binding of nar3 but not that of RRV. These results suggest that while RRV binds to the cell through VP8, the variant does so through the VP5 domain of VP4. This observation was further sustained by the fact that recombinant VP8 and VP5 proteins, produced in bacteria as fusion products with glutathione S-transferase, were found to bind to MA104 cells in a specific and saturable manner and, when preincubated with the cell, were capable of inhibiting the binding of wild-type and variant viruses, respectively. In addition, the VP5 and VP8 recombinant proteins inhibited the infectivity of nar3 and RRV, respectively, confirming the results obtained in the binding assays. Interestingly, when the infectivity assay was performed on neuraminidase-treated cells, the VP5 fusion protein was also found to inhibit the infectivity of RRV, suggesting that RRV could bind to the cell through two sequential steps mediated by the interaction of VP8 and VP5 with SA-containing and SA-independent cell surface receptors, respectively.

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