scholarly journals Mapping of conserved and species-specific antibody epitopes on the Ebola virus nucleoprotein

2013 ◽  
Vol 176 (1-2) ◽  
pp. 83-90 ◽  
Author(s):  
Katendi Changula ◽  
Reiko Yoshida ◽  
Osamu Noyori ◽  
Andrea Marzi ◽  
Hiroko Miyamoto ◽  
...  
Keyword(s):  
Specific Antibody ◽  
Ebola Virus ◽  
Species Specific ◽  
Antibody Epitopes

scholarly journals Ehrlichia canis gp200 Contains Dominant Species-Specific Antibody Epitopes in Terminal Acidic Domains

2007 ◽  
Vol 75 (10) ◽  
pp. 4900-4908 ◽  
Author(s):  
Kimberly A. Nethery ◽  
C. Kuyler Doyle ◽  
Xiaofeng Zhang ◽  
Jere W. McBride
Keyword(s):  
Amino Acids ◽  
Specific Antibody ◽  
Amino Acid Content ◽  
Ehrlichia Canis ◽  
Biophysical Properties ◽  
B Cell Epitopes ◽  
Immunoreactive Protein ◽  
Recombinant Polypeptides ◽  
Species Specific ◽  
Antibody Epitopes

ABSTRACT Species-specific antibody epitopes within several major immunoreactive protein orthologs of Ehrlichia species have recently been identified and molecularly characterized. In this study, dominant B-cell epitopes within the acidic (pI 5.35) ankyrin repeat-containing 200-kDa major immunoreactive protein (gp200) of Ehrlichia canis were defined. The E. canis gp200 gene (4,263 bp; 1,421 amino acids) was cloned and expressed as four (N-terminal, 1,107 bp; N-internal, 910 bp; C-internal, 1,000 bp; and C-terminal, 1,280 bp) overlapping recombinant proteins. The N-terminal, C-internal, and C-terminal polypeptides (369, 332, and 426 amino acids, respectively) were strongly recognized by antibody, and the major epitope(s) in these polypeptides was mapped to four polypeptide regions (40 to 70 amino acids). Smaller overlapping recombinant polypeptides (14 to 15 amino acids) spanning these regions identified five strongly immunoreactive species-specific epitopes that exhibited conformational dependence. The majority of the epitopes (four) were located in two strongly acidic (pI 4 to 4.9) domains in the distal N- and C-terminal regions of the protein flanking the centralized ankyrin domain-containing region. The amino acid content of the epitope-containing domains included a high proportion of strongly acidic amino acids (glutamate and aspartate), and these domains appear to have important biophysical properties that influence the antibody response to gp200.

Fusobacterium varium localized in the colonic mucosa of patients with ulcerative colitis stimulates species-specific antibody

2002 ◽  
Vol 17 (8) ◽  
pp. 849-853 ◽  
Author(s):  
Toshifumi Ohkusa ◽  
Nobuhiro Sato ◽  
Tatuo Ogihara ◽  
Koji Morita ◽  
Masayuki Ogawa ◽  
...  
Keyword(s):  
Ulcerative Colitis ◽  
Specific Antibody ◽  
Colonic Mucosa ◽  
Species Specific ◽  
Fusobacterium Varium

scholarly journals Immunoglobulin G enzyme-linked immunosorbent assay using truncated nucleoproteins of Reston Ebola virus

2003 ◽  
Vol 130 (3) ◽  
pp. 533-539 ◽  
Author(s):  
T. IKEGAMI ◽  
M. SAIJO ◽  
M. NIIKURA ◽  
M. E. MIRANDA ◽  
A. B. CALAOR ◽  
...  
Keyword(s):  
Amino Acid ◽  
Immunosorbent Assay ◽  
Specific Antibody ◽  
Immunoglobulin G ◽  
Ebola Virus ◽  
Enzyme Linked Immunosorbent Assay ◽  
Cynomolgus Macaques

We developed an immunoglobulin G (IgG) enzyme-linked immunosorbent assay (ELISA), using partial recombinant nucleoproteins (rNP) of Reston Ebola virus (EBO-R) and Zaire Ebola virus (EBO-Z). We examined the reaction of 10 sera from cynomolgus macaques naturally infected with EBO-R to each of the partial rNP in the IgG ELISA. All the sera reacted to the C-terminal halves of the rNP of both EBO-R and EBO-Z. Most of the sera reacted to the RΔC (amino acid (aa) 360–739), and RΔ6 (aa 451–551) and/or RΔ8 (aa 631–739) at a higher dilution than to the corresponding truncated rNPs of EBO-Z. The results indicate that this IgG ELISA is useful for detecting EBO-R specific antibody, and may have a potential to discriminate EBO-R infection from other subtypes.

Use of a species-specific antibody for demonstrating mouse neurons transplanted to rat brains

1985 ◽  
Vol 61 (1-2) ◽  
pp. 221-226 ◽  
Author(s):  
R.D. Lund ◽  
F.-L.F. Chang ◽  
M.H. Hankin ◽  
C.F. Lagenaur
Keyword(s):  
Specific Antibody ◽  
Species Specific

scholarly journals Influences of Glycosylation on Antigenicity, Immunogenicity, and Protective Efficacy of Ebola Virus GP DNA Vaccines

2006 ◽  
Vol 81 (4) ◽  
pp. 1821-1837 ◽  
Author(s):  
William Dowling ◽  
Elizabeth Thompson ◽  
Catherine Badger ◽  
Jenny L. Mellquist ◽  
Aura R. Garrison ◽  
...  
Keyword(s):  
T Cell ◽  
Protective Immunity ◽  
Ebola Virus ◽  
Dna Vaccines ◽  
Protective Efficacy ◽  
T Cell Epitopes ◽  
Glycosylation Sites ◽  
Membrane Bound ◽  
Antibody Epitopes

ABSTRACT The Ebola virus (EBOV) envelope glycoprotein (GP) is the primary target of protective immunity. Mature GP consists of two disulfide-linked subunits, GP1 and membrane-bound GP2. GP is highly glycosylated with both N- and O-linked carbohydrates. We measured the influences of GP glycosylation on antigenicity, immunogenicity, and protection by testing DNA vaccines comprised of GP genes with deleted N-linked glycosylation sites or with deletions in the central hypervariable mucin region. We showed that mutation of one of the two N-linked GP2 glycosylation sites was highly detrimental to the antigenicity and immunogenicity of GP. Our data indicate that this is likely due to the inability of GP2 and GP1 to dimerize at the cell surface and suggest that glycosylation at this site is required for achieving the conformational integrity of GP2 and GP1. In contrast, mutation of two N-linked sites on GP1, which flank previously defined protective antibody epitopes on GP, may enhance immunogenicity, possibly by unmasking epitopes. We further showed that although deleting the mucin region apparently had no effect on antigenicity in vitro, it negatively impacted the elicitation of protective immunity in mice. In addition, we confirmed the presence of previously identified B-cell and T-cell epitopes in GP but show that when analyzed individually none of them were neither absolutely required nor sufficient for protective immunity to EBOV. Finally, we identified other potential regions of GP that may contain relevant antibody or T-cell epitopes.

Detection of species-specific antibody response of humans and mice bitten by sand flies

Parasitology ◽  
2005 ◽  
Vol 130 (5) ◽  
pp. 493-499 ◽  
Author(s):  
I. ROHOUSOVA ◽  
S. OZENSOY ◽  
Y. OZBEL ◽  
P. VOLF
Keyword(s):  
Antibody Response ◽  
Specific Antibody ◽  
Sand Flies ◽  
Specific Antibody Response ◽  
Species Specific

scholarly journals Zoonotic potential of a novel bat morbillivirus

2021 ◽  
Author(s):  
Satoshi Ikegame ◽  
Jillian C Carmichael ◽  
Heather Wells ◽  
Robert L Furler ◽  
Joshua A Acklin ◽  
...  
Keyword(s):  
Measles Virus ◽  
Reverse Genetics ◽  
Ebola Virus ◽  
Severe Disease ◽  
Nipah Virus ◽  
Lymphoid Cells ◽  
Zoonotic Potential ◽  
Specific Expression ◽  
Animal Populations ◽  
Species Specific

Bats are significant reservoir hosts for many viruses with zoonotic potential. SARS-CoV-2, Ebola virus, and Nipah virus are examples of such viruses that have caused deadly epidemics and pandemics when spilled over from bats into human and animal populations. Careful surveillance of viruses in bats is critical for identifying potential zoonotic pathogens. However, metagenomic surveys in bats often do not result in full-length viral sequences that can be used to regenerate such viruses for targeted characterization. Here, we identify and characterize a novel morbillivirus from a vespertilionid bat species (Myotis riparius) in Brazil, which we term myotis bat morbillivirus (MBaMV). There are 7 species of morbilliviruses including measles virus (MeV), canine distemper virus (CDV) and rinderpest virus (RPV). All morbilliviruses cause severe disease in their natural hosts, and pathogenicity is largely determined by species specific expression of canonical morbillivirus receptors, CD150/SLAMF1 and NECTIN4. MBaMV used Myotis spp CD150 much better than human and dog CD150 in fusion assays. We confirmed this using live MBaMV that was rescued by reverse genetics. Surprisingly, MBaMV replicated efficiently in primary human myeloid but not lymphoid cells. Furthermore, MBaMV replicated in human epithelial cells and used human NECTIN4 almost as well as MeV. Our results demonstrate the unusual ability of MBaMV to infect and replicate in some human cells that are critical for MeV pathogenesis and transmission. This raises the specter of zoonotic transmission of a bat morbillivirus.

Immunoreactive Protein Repertoires of Ehrlichia chaffeensis and E. canis Reveal the Dominance of Hypothetical Proteins and Conformation-dependent Antibody Epitopes

2021 ◽  
Author(s):  
Tian Luo ◽  
Jignesh G. Patel ◽  
Xiaofeng Zhang ◽  
David H. Walker ◽  
Jere W. McBride
Keyword(s):  
Immune Responses ◽  
Hypothetical Protein ◽  
Ehrlichia Chaffeensis ◽  
Hypothetical Proteins ◽  
Significant Group ◽  
Molecular Features ◽  
A Genome ◽  
Species Specific ◽  
Protective Proteins ◽  
Antibody Epitopes

The immunomes of Ehrlichia chaffeensis ( E. ch. ) and E. canis ( E. ca. ) have recently be revised to include immunodominant hypothetical proteins with conformational antibody epitopes. In this study, we examined 216 E. ch. and 190 E. ca. highly antigenic proteins according to ANTIGENpro and also performed a genome-wide hypothetical protein analysis ( E. ch. n=104; E. ca. n=124) for immunoreactivity. Using cell-free protein expression and immunoanalysis, 118 E. ch. and 39 E. ca . proteins reacted with sera from naturally E. ch. -infected patients or E. ca. -infected dogs. Moreover, 22 E. ch. and 18 E. ca. proteins consistently and strongly reacted with a panel of patient or canine sera. A subset of E. ch. (n=18) and E. ca. (n=9) proteins were identified as immunodominant. Consistent with our previous study, most proteins were classified as hypothetical and the antibody epitopes exhibited complete or partial conformation-dependence. The majority (28/40; 70%) of E. ch. and E. ca. proteins contained transmembrane domains and 19 (48%) were predicted to be secreted effectors. The antigenic repertoires of E. ch. and E. ca. were mostly diverse and suggest that the immunomes of these closely related ehrlichiae are dominated by species-specific conformational antibody epitopes. This study reveals a significant group of previously undefined E. ch. and E. ca. antigens and reaffirms the importance of conformation-dependent epitopes as targets of anti- Ehrlichia immune responses. These findings substantially expand our understanding of host- Ehrlichia immune responses, advance efforts to define the molecular features of protective proteins and improve prospects for effective vaccines for the ehrlichioses.

scholarly journals Species-Specific Antibody Responses to the Recombinant 53-Kilodalton Excretory and Secretory Proteins in Mice Infected with Trichinella spp.

2008 ◽  
Vol 15 (3) ◽  
pp. 468-473 ◽  
Author(s):  
Isao Nagano ◽  
Zhiliang Wu ◽  
Yuzo Takahashi
Keyword(s):  
Escherichia Coli ◽  
Recombinant Protein ◽  
Recombinant Proteins ◽  
Specific Antibody ◽  
Expression System ◽  
Amino Acid Sequences ◽  
Antibody Responses ◽  
Secretory Proteins ◽  
Muscle Larvae ◽  
Species Specific

ABSTRACT The 53-kDa proteins in larval excretory and secretory (E-S) products were expressed from five Trichinella species (T. spiralis, T. britovi, T. nativa, T. pseudospiralis, and T. papuae), using the Escherichia coli expression system, and the antibody responses to the 53-kDa recombinant proteins in mice infected with Trichinella spp. were analyzed by Western blotting. The 53-kDa protein is conserved among the five Trichinella species, with >60% similarity in amino acid sequences. The 53-kDa recombinant proteins of T. spiralis and T. pseudospiralis reacted to sera from mice infected with T. spiralis and T. pseudospiralis at 8 days postinfection (p.i.), respectively. An antibody against the 53-kDa recombinant protein of T. spiralis recognized the 53-kDa protein in the crude extracts from adult worms and 30-day p.i. muscle larvae and E-S products from muscle larvae of T. spiralis but did not recognize any proteins from T. pseudospiralis. The sera from the mice infected with T. spiralis strongly reacted with the 53-kDa recombinant protein of T. spiralis but did not react with the 53-kDa recombinant proteins of T. britovi, T. nativa, T. pseudospiralis, and T. papuae. Similarly, the sera from mice infected with T. britovi, T. nativa, T. pseudospiralis, or T. papuae strongly reacted with the 53-kDa recombinant proteins of T. britovi, T. nativa, T. pseudospiralis, or T. papuae, respectively. These results showed that the 53-kDa recombinant proteins provide early and species-specific antibody responses in mice infected with Trichinella spp.

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