Amino acid sequence requirements for the epitope recognized by a monoclonal antibody reacting with the secreted antigen GP28.5 of Toxoplasma gondii

1992 ◽  
Vol 29 (11) ◽  
pp. 1375-1382 ◽  
Author(s):  
M.F. Cesbron-Delauw ◽  
C. Boutillon ◽  
C. Mercier ◽  
M.P. Fourmaux ◽  
A. Murray ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Amino Acid ◽  
Toxoplasma Gondii ◽  
Amino Acid Sequence ◽  
Sequence Requirements

Identification and cDNA cloning of a Xenopus nucleolar phosphoprotein, xNopp180, that is the homolog of the rat nucleolar protein Nopp140

1995 ◽  
Vol 108 (10) ◽  
pp. 3339-3347 ◽  
Author(s):  
C. Cairns ◽  
B. McStay
Keyword(s):  
Monoclonal Antibody ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Cloning ◽  
Cdna Clone ◽  
Xenopus Oocyte ◽  
Ribosome Biogenesis ◽  
Nucleolar Protein ◽  
Nuclear Localisation Signal ◽  
Cdc2 Kinase

The monoclonal antibody G1C7, recognises both Xenopus nucleolin and a protein of 180 kDa present in Xenopus oocyte nucleoli. This antibody was used to obtain a cDNA clone encoding the 180 kDa protein now called xNopp180 (Xenopus nucleolar phosphoprotein of 180 kDa). Analysis of the deduced amino acid sequence from this cDNA shows that xNopp180 is almost entirely composed of alternating acidic and basic domains. We show that xNopp180 is heavily phosphorylated and that it contains multiple consensus sites for phosphorylation by casein kinase II and cdc2 kinase. In addition we show that xNopp180 is the 180 kDa antigen recognised by the monoclonal antibody No-114, thus allowing reinterpretation of previous work with this antibody. xNopp180 appears to be the Xenopus homolog of the rat nucleolar protein Nopp140. Nopp140 is a nuclear localisation signal binding protein that shuttles on curvilinear tracks between the nucleolus and the cytoplasm. Possible roles for xNopp180/Nopp140 in ribosome biogenesis are discussed.

scholarly journals A monoclonal antibody that defines an idiotope with two subsites in galactan-binding myeloma proteins.

1981 ◽  
Vol 154 (6) ◽  
pp. 1946-1956 ◽  
Author(s):  
M Pawlita ◽  
E Mushinski ◽  
R J Feldmann ◽  
M Potter
Keyword(s):  
Monoclonal Antibody ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Data ◽  
Molecular Models ◽  
Myeloma Protein ◽  
Amino Acid Sequence Data ◽  
Myeloma Proteins ◽  
Igg1 Monoclonal Antibody ◽  
Hybridoma Technology

An IgG1 monoclonal antibody HyX24-14 was derived from A/J mice that were immunized with the IgA XRPC24 (X24) galactan binding myeloma protein (GalBMP) of BALB/c origin by the Kohler-Milstein hybridoma technology. HyX24-14 specifically binds some but all GalBMP. Different patterns of binding using a panel of nine Gal BMP were found, depending upon the concentration of antibody and the antigenic target. From molecular models and amino acid sequence data, ti was proposed that the idiotope defined by HyX24-14 had two subsites, each of which appeared to be able to bind independently to the antibody.

scholarly journals Cloning of the Gene Encoding the Actinobacillus actinomycetemcomitans Serotype b OmpA-Like Outer Membrane Protein

1999 ◽  
Vol 67 (2) ◽  
pp. 942-945 ◽  
Author(s):  
Hitoshi Komatsuzawa ◽  
Toshihisa Kawai ◽  
Mark E. Wilson ◽  
Martin A. Taubman ◽  
Motoyuki Sugai ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Amino Acid ◽  
Membrane Protein ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Actinobacillus Actinomycetemcomitans ◽  
Gene Encoding ◽  
Serotype B

ABSTRACT The gene encoding an outer membrane protein A (OmpA)-like, heat-modifiable Omp of Actinobacillus actinomycetemcomitans ATCC 43718 (strain Y4, serotype b) was cloned by a PCR cloning procedure. DNA sequence analysis revealed that the gene encodes a protein of 346 amino acid residues with a molecular mass of 36.9 kDa. The protein expressed by the cloned gene reacted with a monoclonal antibody to the previously described 29-kDa Omp (Omp29) of strain Y4. This monoclonal antibody reacted specifically with Omp29 of A. actinomycetemcomitans (serotype b), but not with any Omp of Escherichia coli, including OmpA. This protein exhibited characteristic heat modifiability on sodium dodecyl sulfate-polyacrylamide gels, showing an apparent molecular mass of 29 kDa when unheated and a mass of 34 kDa when heated. The N-terminal amino acid sequence of the protein expressed inE. coli perfectly matched those deduced from the purified Omp29 of strain Y4. The deduced amino acid sequence of the gene coding for Omp29 from serotype b matched completely (except for valine at position 321) that of a recently reported omp34gene described for A. actinomycetemcomitans serotype c (NCTC 9710). Because of the conserved nature of the gene within these serotypes, we designated the gene described herein from serotype b asomp34.

scholarly journals Amino Acid Sequence Requirements of the Transmembrane and Cytoplasmic Domains of Influenza Virus Hemagglutinin for Viable Membrane Fusion

1999 ◽  
Vol 10 (6) ◽  
pp. 1821-1836 ◽  
Author(s):  
Grigory B. Melikyan ◽  
Sasa Lin ◽  
Michael G. Roth ◽  
Fredric S. Cohen
Keyword(s):  
Influenza Virus ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Membrane Fusion ◽  
Integral Membrane Protein ◽  
Wild Type ◽  
Influenza Virus Hemagglutinin ◽  
Tm Domain ◽  
Fusion Pores ◽  
Sequence Requirements

The amino acid sequence requirements of the transmembrane (TM) domain and cytoplasmic tail (CT) of the hemagglutinin (HA) of influenza virus in membrane fusion have been investigated. Fusion properties of wild-type HA were compared with those of chimeras consisting of the ectodomain of HA and the TM domain and/or CT of polyimmunoglobulin receptor, a nonviral integral membrane protein. The presence of a CT was not required for fusion. But when a TM domain and CT were present, fusion activity was greater when they were derived from the same protein than derived from different proteins. In fact, the chimera with a TM domain of HA and truncated CT of polyimmunoglobulin receptor did not support full fusion, indicating that the two regions are not functionally independent. Despite the fact that there is wide latitude in the sequence of the TM domain that supports fusion, a point mutation of a semiconserved residue within the TM domain of HA inhibited fusion. The ability of a foreign TM domain to support fusion contradicts the hypothesis that a pore is composed solely of fusion proteins and supports the theory that the TM domain creates fusion pores after a stage of hemifusion has been achieved.

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