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Found 3 matching records:

Displaying record number 925

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MAb ID	F1
HXB2 Location	Nef(148-157) DNA(9238..9267)	Nef Epitope Map
Author Location	Nef(148-157 IIIB)
Epitope	`VEPDKVEEAN`	Epitope Alignment
Ab Type
Neutralizing
Species (Isotype)	mouse(IgM)
Patient
Immunogen
Keywords

Notes

Showing 4 of 4 notes.

F1 database comment: There is a Nef (Fujii1993) and a CD4BS (Haynes2005) MAb that are called F1.
F1: A carboxy-terminal domain of Nef on the cell surface induces cytolysis of CD4+ T cells. Fujii1996b
F1: Insect cells expressing myristylated Nef proteins on their cell surface can induce cytolysis of unstimulated CD4+ cells -- this response is not due to MHC restricted CTL activity -- the cell surface of Nef expressing insect cells carry Nef that can be recognized by MAbs E7 and E9 but not F1. Fujii1996
F1: The C-term end of Nef is accessible to Abs at the cell surface -- stained IIIB/M10, but not MN/M10, cells. Fujii1993,Otake1994

References

Showing 4 of 4 references.

Fujii1993 Y. Fujii, Y. Nishino, T. Nakaya, K. Tokunaga, and K. Ikuta. Expression of Human Immunodeficiency Virus Type 1 Nef Antigen on the Surface of Acutely and Persistently Infected Human T-cells. Vaccine, 11:1240, 1993. PubMed ID: 8256505. Show all entries for this paper.

Fujii1996 Y. Fujii, K. Otake, M. Tashiro, and A. Adachi. In Vitro Cytocidal Effects of Human Immunodeficiency Virus Type 1 Nef on Unprimed Human CD4+ T Cells without MHC Restriction. J. Gen. Virol., 77:2943-2951, 1996. PubMed ID: 9000084. Show all entries for this paper.

Fujii1996b Y. Fujii, K. Otake, M. Tashiro, and A. Adachi. Human Immunodeficiency Type 1 Nef Protein on the Cell Surface Is Cytocidal for Human CD4+ T cells. FEBS Lett., 393:105-108, 1996. PubMed ID: 8804435. Show all entries for this paper.

Otake1994 K. Otake, Y. Fujii, Y. Nishino, Q. Zhong, K. Fujinaga, M. Kameoka, K. Ohki, and K. Ikuta. The Carboxyl-Terminal Region of HIV-1 Nef Protein Is a Cell Surface Domain That Can Interact with CD4+ T Cells. J. Immunol., 153:5826-5837, 1994. This study shows that the C-terminal end of Nef is accessible to Abs. This domain could bind in a soluble form to CD4+, uninfected cells, and this interaction is inhibited in the presence of the C-terminal specific antibodies. Syncytium formation was reduced by these Abs or peptides. Abs could stain IIIB/M10, but not MN/M10, infected cells, in a membrane immunofluorescence assay. PubMed ID: 7989778. Show all entries for this paper.

Displaying record number 927

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MAb ID	E9
HXB2 Location	Nef(158-181) DNA(9268..9339)	Nef Epitope Map
Author Location	Nef(158-206 IIIB)
Epitope	`KGENTSLLHPVSLHGMDDPEREVL`	Epitope Alignment
Ab Type
Neutralizing
Species (Isotype)	mouse(IgM)
Patient
Immunogen
Keywords

Notes

Showing 4 of 4 notes.

E9: This epitope is similar to a fragment of the human protein Hematopoietic progenitor cell antigen CD34, TSLHPVSQHG. Maksiutov2002
E9: Insect cells expressing myristylated Nef proteins on their cell surface can induce cytolysis of unstimulated CD4+ cells -- this response is not due to MHC restricted CTL activity -- the cell surface of Nef expressing insect cells carry Nef that can be recognized by MAbs E7 and E9 but not F1. Fujii1996
E9: A carboxy-terminal domain of Nef on the cell surface induces cytolysis of CD4+ T cells. Fujii1996b
E9: The C-term end of Nef is accessible to Abs at the cell surface -- stained IIIB/M10, but not MN/M10, cells. Fujii1993,Otake1994

References

Showing 5 of 5 references.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.

Displaying record number 934

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MAb ID	E7
HXB2 Location	Nef(192-206) DNA(9370..9414)	Nef Epitope Map
Author Location	Nef(192-206 IIIB)
Epitope	`HHVARELHPEYFKNC`	Epitope Alignment
Ab Type
Neutralizing
Species (Isotype)	mouse(IgM)
Patient
Immunogen
Keywords

Notes

Showing 5 of 5 notes.

E7: Soluble Nef inhibits proliferation of CD4+ cells, and Nef cross-linking by MAbs may induce anti-CD4 cytocidal activity -- sera from HIV+ individuals contain soluble Nef, thus this may be important for immune dysfunction and disease progression. Fujii1996c
E7: A carboxy-terminal domain of Nef on the cell surface induces cytolysis of CD4+ T cells. Fujii1996b
E7: Nef forms a homomeric oligomerizing structure, and using E7 and membrane immunofluorescence or immunoelectron microscopy, was shown to clusters on the surface of HIV-1 infected CD4+ cells. Fujii1996a
E7: Insect cells expressing myristylated Nef proteins on their cell surface can induce cytolysis of unstimulated CD4+ cells -- this response is not due to MHC restricted CTL activity -- the cell surface of Nef expressing insect cells carry Nef that can be recognized by MAbs E7 and E9 but not F1. Fujii1996
E7: The C-term end of Nef is accessible to Abs at the cell surface -- stained IIIB/M10, but not MN/M10, cells. Fujii1993,Otake1994

References

Showing 6 of 6 references.

Fujii1996a Y. Fujii, K. Otake, Y. Fujita, N. Yamaimoto, Y. Nagai, M. Tashiro, and A. Adachi. Clustered Localization of Oligomeric Nef Protein of Human Immunodeficiency Virus Type 1 on the Cell Surface. FEBS Lett., 395:257-261, 1996. PubMed ID: 8898107. Show all entries for this paper.

Fujii1996c Y. Fujii, K. Otake, M. Tashiro, and A. Adachi. Soluble Nef Antigen of HIV-1 Is Cytotoxic for Human CD4+ T Cells. FEBS Lett., 393:93-96, 1996. PubMed ID: 8804432. Show all entries for this paper.