scholarly journals The Carboxy Terminal Region on Spike Protein of Porcine Epidemic Diarrhea Virus (PEDV) Is Important for Evaluating Neutralizing Activity

Pathogens ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 683
Author(s):  
Ki-Jong Kang ◽  
Dong-Hwan Kim ◽  
Eui-Ju Hong ◽  
Hyun-Jin Shin
Keyword(s):  
Vaccine Efficacy ◽  
Terminal Region ◽  
Enzyme Linked Immunosorbent Assay ◽  
Neutralizing Epitope ◽  
Nucleocapsid Proteins ◽  
S Protein ◽  
Neutralizing Activity ◽  
Diarrhea Virus ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal

In this study, we evaluated 62 sow sera samples from PED-vaccinated sows to compare the serum neutralizing test (SNT) and enzyme-linked immunosorbent assay (ELISA). We performed protein ELISA (pELISA) using fragments of spike proteins S1, S2, S3 and entire nucleocapsid proteins, and found a correlation between the SNT and ELISA in PEDV-vaccinated sera. Sera with higher neutralizing activity showed higher titers of IgG. In the antibody profiling, the neutralizing activities are correlated with the levels of the spike antibody, especially the S3 region. We confirmed that the carboxy-terminal region, including the endodomain of the S protein, induced stronger neutralizing activity than the ectodomain. This region of the S protein could be useful for evaluating PED vaccine efficacy, and it is a strong neutralizing epitope of PEDV. The S3 protein could be useful for evaluating PED vaccine efficacy, and it is a strong neutralizing epitope of PEDV.

scholarly journals The Carboxy-Terminal Region of apoA-I Is Required for the ABCA1-Dependent Formation of α-HDL But Not Preβ-HDL Particles in Vivo†

Biochemistry ◽  
2007 ◽  
Vol 46 (19) ◽  
pp. 5697-5708 ◽  
Author(s):  
Angeliki Chroni ◽  
Georgios Koukos ◽  
Adelina Duka ◽  
Vassilis I. Zannis
Keyword(s):  
Terminal Region ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal

Tubulin folding is altered by mutations in a putative GTP binding motif

1996 ◽  
Vol 109 (6) ◽  
pp. 1471-1478 ◽  
Author(s):  
J.C. Zabala ◽  
A. Fontalba ◽  
J. Avila
Keyword(s):  
Intramolecular Interaction ◽  
Terminal Region ◽  
Binding Motif ◽  
Beta Tubulin ◽  
Alpha Tubulin ◽  
Proposed Model ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal ◽  
Hydrolysis Of

Tubulins contain a glycine-rich loop, that has been implicated in microtubule dynamics by means of an intramolecular interaction with the carboxy-terminal region. As a further extension of the analysis of the role of the carboxy-terminal region in tubulin folding we have mutated the glycine-rich loop of tubulin subunits. An alpha-tubulin point mutant with a T150-->G substitution (the corresponding residue present in beta-tubulin) was able to incorporate into dimers and microtubules. On the other hand, four beta-tubulin point mutants, including the G148-->T substitution, did not incorporate into dimers, did not release monomers, but were able to form C900 and C300 complexes (intermediates in the process of tubulin folding). Three other mutants within this region (which approximately encompasses residues 137–152) were incapable of forming dimers and C300 complexes but gave rise to the formation of C900 complexes. These results suggest that tubulin goes through two sequential folding states during the folding process, first in association with TCP1-complexes (C900) prior to the transfer to C300 complexes. It is this second step that implies binding/hydrolysis of GTP, reinforcing our previous proposed model for tubulin folding and assembly.

scholarly journals THE DISTRIBUTION OF ANTIGENIC DETERMINANTS IN RAT SKIN COLLAGEN

1971 ◽  
Vol 133 (6) ◽  
pp. 1309-1324 ◽  
Author(s):  
Herbert Lindsley ◽  
Mart Mannik ◽  
Paul Bornstein
Keyword(s):  
Terminal Region ◽  
Antigenic Determinants ◽  
Collagen Molecule ◽  
Rat Skin ◽  
Amino Terminal ◽  
Skin Collagen ◽  
Native Collagen ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal ◽  
Hyperimmune Rabbit

Immunological studies of rat skin collagen were carried out with a sensitive and quantitative radioimmunoassay. Hyperimmune rabbit antisera to rat skin collagen and isolated α2 chains were used. Iodine-labeled α chains and CNBr-produced peptides served as test antigens, and native collagen, α chains, and CNBr peptides were employed as inhibitors in the assay. The α1 and α2 chains were immunologically distinct. Although the α1 chain was not immunogenic, antibodies to α1 were detected in antisera to the intact collagen molecule. The major antigenic determinant of the α1 chain was located in α1-CB6 which constitutes the carboxy-terminal region of the chain. The α2 chain contained two non-cross-reacting antigenic determinants, one in the amino-terminal region (α2-CB1) and the other in the carboxy-terminal region (α2-CB5) of the chain. The native collagen molecule was less effective than isolated α chains in inhibiting binding of labeled peptides to antisera, indicating that antigenic determinants were less accessible in the triple helical molecule. These immunologic studies are consistent with preliminary comparative biochemical data which indicate that interspecies structural differences in collagen predominate at both the amino- and carboxy-terminal ends of the chains.

scholarly journals Carboxy-Terminal Region Involved in Activity of Escherichia coli TolC

2001 ◽  
Vol 183 (23) ◽  
pp. 6961-6964 ◽  
Author(s):  
Hiroyasu Yamanaka ◽  
Hiroshi Izawa ◽  
Keinosuke Okamoto
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Outer Membrane ◽  
Amino Acid Residue ◽  
Terminal Region ◽  
Transport Activity ◽  
Carboxy Terminus ◽  
Partial Deletion ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal

ABSTRACT The Escherichia coli TolC acts as a channel tunnel in the transport of various molecules across the outer membrane. Partial-deletion studies of tolC revealed that the region extending from the 50th to the 60th amino acid residue from the carboxy terminus plays an important role in this transport activity of TolC.

The Carboxy-Terminal Region of Sturgeon Muscle Aldolase

1971 ◽  
Vol 49 (3) ◽  
pp. 372-375
Author(s):  
P. J. Anderson
Keyword(s):  
Amino Acids ◽  
Terminal Region ◽  
Rabbit Muscle ◽  
Muscle Enzyme ◽  
Molar Ratios ◽  
Carboxy Terminal Region ◽  
Kinetic Effects ◽  
Carboxy Terminal ◽  
Similar Kinetic

The modification of the carboxy-terminal of sturgeon muscle aldolase with carboxypeptidase produces similar kinetic effects to those observed on modification of the rabbit muscle enzyme. The nature and molar ratios of amino acids released indicate that differences between the two enzymes occur in the carboxy-terminal region.

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