B-cell epitopes of the Nef protein

Spohn, Renate; Gombert, Frank O.; Jung, Günther

doi:10.1016/s0923-2516(06)80085-3

Cited by 4 publications

(4 citation statements)

References 27 publications

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“…AUTODISPLAY ON THE E. COLI CELL SURFACE 797 monoclonal antibody Dü142 (42). For this purpose, we constructed plasmid pJM22, which encodes fusion protein FP50 exhibiting a molecular mass of 49.7 kDa (Fig.…”

Section: Vol 179 1997mentioning

confidence: 99%

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Autodisplay: one-component system for efficient surface display and release of soluble recombinant proteins from Escherichia coli

1997

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The immunoglobulin A protease family of secreted proteins are derived from self-translocating polyprotein precursors which contain C-terminal domains promoting the translocation of the N-terminally attached passenger domains across gram-negative bacterial outer membranes. Computer predictions identified the C-terminal domain of the Escherichia coli adhesin involved in diffuse adherence (AIDA-I) as a member of the autotransporter family. A model of the ␤-barrel structure, proposed to be responsible for outer membrane translocation, served as a basis for the construction of fusion proteins containing heterologous passengers. Autotransporter-mediated surface display (autodisplay) was investigated for the cholera toxin B subunit and the peptide antigen tag PEYFK. Up to 5% of total cellular protein was detectable in the outer membrane as passenger autotransporter fusion protein synthesized under control of the constitutive P TK promoter. Efficient presentation of the passenger domains was demonstrated in the outer membrane protease T-deficient (ompT) strain E. coli UT5600 and the ompT dsbA double mutant JK321. Surface exposure was ascertained by enzyme-linked immunosorbent assay, immunofluorescence microscopy, and immunogold electron microscopy using antisera specific for the passenger domains. In strain UT2300 (ompT ؉ ), the passenger domains were released from the cell surface by the OmpT protease at a novel specific cleavage site, R2V. Autodisplay represents a useful tool for future protein translocation studies with interesting biotechnological possibilities.

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Section: Vol 179 1997mentioning

confidence: 99%

“…The 5Ј extension of JM20 encoded five amino acids (PEYFK) that are recognized as a linear epitope by monoclonal antibody Dü142 (42). The PCR product was digested with KpnI and circularized to yield pJM22.…”

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confidence: 99%

Autodisplay: one-component system for efficient surface display and release of soluble recombinant proteins from Escherichia coli

1997

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“…Two binding regions are located in the C-terminal portion of Nef (aa 175-190 and 86-166), whereas the third epitope (aa 83-93) is located in the middle of the protein overlapping those described by others [14,40,44]. Three of the mabs reacting with recombinant polypeptides as well as with synthetic peptides are most likely directed against sequential epitopes (aa 83-93 and 175-190) which are highly conserved in all HIV-1 strains sequenced so far [33].…”

Section: Discussionmentioning

confidence: 79%

“…In indirect immunofluorescence tests it bound to HIV-1 infected as well as to uninfected T-cells. The proposed epitope overlaps the central region of Nef (aa 90-150) which was shown to induce a strong humoral immune response in humans but described as completely non-reactive with mouse anti-Nef sera [44]. Most interesting features of Nef are its similarity to a number of signal transducing proteins, in particular G proteins, and its ability to down-regulate the CD4-cell surface expression.…”

Section: Discussionmentioning

confidence: 99%

Fine mapping of HIV-1 Nef-epitopes by monoclonal antibodies

Siakkou

Jahn

Kienzle

et al. 1993

Archives of Virology

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A panel of newly isolated murine monoclonal antibodies is described which are specific for the Nef protein of the human immunodeficiency virus type 1 (HIV-1). Epitope mapping using recombinant Nef-related proteins, synthetic peptides and lipopeptides showed 3 independent antigenic determinants located within the regions of amino acids 83-93, 175-190 and 86-166 of the Nef protein. None of the monoclonal antibodies reacted with recombinant Nef proteins of HIV-2.

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Peptide presentation by major histocompatibility complex-class I and in vivo induction of cytotoxic T-lymphocytes

Jung¹

1993

Peptide Chemistry 1992

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B-cell epitopes of the Nef protein

Cited by 4 publications

References 27 publications

Autodisplay: one-component system for efficient surface display and release of soluble recombinant proteins from Escherichia coli

Autodisplay: one-component system for efficient surface display and release of soluble recombinant proteins from Escherichia coli

Fine mapping of HIV-1 Nef-epitopes by monoclonal antibodies

Peptide presentation by major histocompatibility complex-class I and in vivo induction of cytotoxic T-lymphocytes

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