Surface Plasmon Resonance Analysis of gp17, a Natural CD4 Ligand from Human Seminal Plasma Inhibiting Human Immunodeficiency Virus Type‐1 gp120‐Mediated Syncytium Formation

Autiero, Monica; Gaubin, Muriel; Mani, Jean‐Claude; Castejon, Christophe; Martín, M.V.; Marhomy, Sandrine El; Guardiola, John; Piatier‐Tonneau, Dominique

doi:10.1111/j.1432-1033.1997.00208.x

Cited by 45 publications

(32 citation statements)

References 39 publications

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“…Earlier reports showed that PIP bind strongly with Fc fragment of IgG (Antisperm Antibody) and CD4 [22,43]. This finding indicates that presumably PIP also has strong affinity for ZAG.…”

Section: Discussionmentioning

confidence: 65%

Purification and characterization of zinc α2‐glycoprotein‐Prolactin inducible protein complex from human seminal plasma

Hassan

Kumar

Singh

et al. 2008

J of Separation Science

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Zinc alpha2-glycoprotein (ZAG) is present at high concentration in human seminal plasma, and considered as soluble homologue of MHC-I. ZAG is a well-known biomarker for prostate and breast carcinomas. We have purified a naturally occurring complex of ZAG with Prolactin inducible protein (PIP), which is also a well-known biomarker for the same. The ZAG-PIP complex has been isolated and purified by simple chromatographic techniques in a reproducible two-step process, using ion exchange and gel-permeation chromatography and subsequently identified by MS. The complex between ZAG and PIP is formed by non-covalent interactions. The purity and molecular mass was determined by SDS-PAGE, which shows the bands corresponding to 40 kDa and 14 kDa, which were also confirmed by MALDI-TOF. Dynamic light scattering (DLS) experiments also showed hydrodynamic radii corresponding to 54, 40 and 14 kDa for ZAG-PIP complex, ZAG and PIP respectively. The concentration dependent aggregation of this complex has also been observed. Fluorescence analysis reveals that complexes have similar binding affinities as native ZAG, for their proposed ligands like arachidonic acid, polyethylene glycol and synthetic peptide. This is the first report on purification and characterization of a naturally occurring complex of ZAG-PIP in human seminal fluid.

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“…Earlier reports showed that PIP bind strongly with Fc fragment of IgG (Antisperm Antibody) and CD4 [22,43]. This finding indicates that presumably PIP also has strong affinity for ZAG.…”

Section: Discussionmentioning

confidence: 65%

Purification and characterization of zinc α2‐glycoprotein‐Prolactin inducible protein complex from human seminal plasma

Hassan

Kumar

Singh

et al. 2008

J of Separation Science

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“…The seminal plasma gp17 binding site on CD4 is also located in the D1 domain, close to but distinct from the gp120-binding site (38).…”

Section: Il-16 Binding Domain On Cd4mentioning

confidence: 94%

Identification of a CD4 Domain Required for Interleukin-16 Binding and Lymphocyte Activation*

Liu¹,

Cruikshank²,

O'Loughlin³

et al. 1999

Journal of Biological Chemistry

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Interleukin-16 (IL-16) activates CD4؉ cells, possibly by direct interaction with CD4. IL-16 structure and function are highly conserved across species, suggesting similar conservation of a putative IL-16 binding site on CD4. Comparison of the human CD4 amino acid sequence with that of several different species revealed that immunoglobulin-like domain 4 is the most conserved extracellular region. Potential interaction of this domain with IL-16 was studied by testing murine D4 sequence-based oligopeptides for inhibition of IL-16 chemoattractant activity and inhibition of IL-16 binding to CD4 in vitro. Three contiguous 12-residue D4 region peptides (designated A, B, and C) blocked IL-16 chemoattractant activity, with peptide B the most potent. Peptides A and B were synergistic for inhibition, but peptide C was not. Peptides A and B also blocked IL-16 binding to CD4 in vitro, whereas peptide C did not. CD4, in addition to its known function as a receptor for major histocompatibility complex class II, contains a binding site for IL-16 in the D4 domain. The D4 residues required for IL-16 binding overlap those previously shown to participate in CD4-CD4 dimerization following class II major histocompatibility complex binding, providing a mechanistic explanation for the known function of IL-16 to inhibit the mixed lymphocyte reaction. 1 was first described in 1982 (1, 2) as lymphocyte chemoattractant factor (LCF). Subsequent studies showed that IL-16 is a multifunctional cytokine, selectively inducing the migration of CD4 ϩ T cells, eosinophils, and monocytes. IL-16 also acts as a growth factor for resting CD4 ϩ T cells, promoting their entry into the G 1 phase of the cell cycle and inducing interleukin-2 receptor and major histocompatibility (MHC) class II protein expression on the cell surface. These activating functions are associated with intracellular signals including the synthesis of inositol trisphosphate and a transient increase of intracellular Ca 2ϩ concentration (reviewed in Ref.3).Previous functional data suggest that CD4 is a receptor for IL-16. IL-16 induces chemotactic responses in CD4 ϩ but not CD4 Ϫ T lymphocytes (4). The T cell chemoattractant response to IL-16 is inhibited by co-incubation with Fab fragments of the anti-CD4 monoclonal antibody OKT 4, and the magnitude of the IL-16-induced cell migration by monocytes is directly proportional to the amount of CD4 expressed on the responding cells (5). Finally, transfection of human CD4 confers IL-16 responsiveness to an otherwise unresponsive L3T4Ϫ murine hybridoma cell line as demonstrated by the induction of cell motility and rises in intracellular Ca 2ϩ and inositol trisphosphate which are inhibited by OKT4 Fab (6). In addition to this functional evidence, there is direct physical evidence for an IL-16-CD4 interaction. IL-16 can be co-immunoprecipitated with recombinant soluble CD4, and rIL-16 partially displaces OKT4 bound to CD4 (7).Data from several laboratories indicate a high degree of sequence and functional homology for IL-16 across different...

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“…The ability of PIP to bind a large array of proteins may account for its multifaceted role in various biological processes, such as fertility, immunoregulation, antimicrobial activity, apoptosis, and tumor progression [20]. In particular, the ability of PIP to bind to CD4 molecule and block CD4-mediated cell programmed death lead to the proposal that it may modulate adaptive immune responses [21][22][23][24][25]. The CD4 molecule plays a critical role in adaptive immunity by acting as a T-cell coreceptor for recognition of peptides bound to MHC class II molecules on APCs [26].…”

Section: Discussionmentioning

confidence: 99%

Deficiency of prolactin‐inducible protein leads to impaired Th1 immune response and susceptibility to Leishmania major in mice

Liu

Mou

et al. 2015

Eur J Immunol

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Although the strategic production of prolactin-inducible protein (PIP) at several ports of pathogen entry into the body suggests it might play a role in host defense, no study has directly implicated it in immunity against any infectious agent. Here, we show for the first time that PIP deficiency is associated with reduced numbers of CD4 + T cells in peripheral lymphoid tissues and impaired CD4 + Th1-cell differentiation in vitro. In vivo, CD4+ T cells from OVA-immunized, PIP-deficient mice showed significantly impaired proliferation and IFN-γ production following in vitro restimulation. Furthermore, PIPdeficient mice were highly susceptible to Leishmani major infection and failed to control lesion progression and parasite proliferation. This susceptibility was associated with impaired NO production and leishmanicidal activity of PIP KO macrophages following IFN-γ and LPS stimulation. Collectively, our findings implicate PIP as an important regulator of CD4 + Th1-cell-mediated immunity. Keywords: IFN-γ r Leishmania r Macrophages r Protozoan r Th1 cellsAdditional supporting information may be found in the online version of this article at the publisher's web-site IntroductionThe mouse prolactin-inducible protein (PIP), also known as the mouse submaxillary gland protein, is a 14 kDa protein present in the saliva of mice. The function of PIP is not known, but it is suspected to play a role in host defense against pathogens [1][2][3][4][5][6] because it is expressed in tissues strategically located at several Correspondence: Dr. Jude E. Uzonna e-mail: jude.uzonna@med.umanitoba.ca ports of pathogen entry, including the skin, eyes, and mouth [7]. Although a definitive evidence showing a role for PIP in host immunity is lacking, its ability to potentially bind with several important host molecules including CD4 + T-cell receptor, IgG, actin, zinc α2-glycoprotein, fibronectin, and enamel pellicle suggests it may have important biological functions [8][9][10][11][12][13]. Indeed, it has been shown that PIP is a ligand of the CD4 molecule and a potent inhibitor of * These authors contributed equally to this manuscript.C 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim www.eji-journal.eu Eur. J. Immunol. 2015. 45: 1082-1091 Immunity to infection 1083 T-cell apoptosis induced by sequential CD4/T-cell receptor triggering, which in part modulates the immune response during viral infection by interfering with the functions mediated by the CD4 molecule [5,6,14]. Furthermore, PIP has been reported to exhibit a mitogenic effect for both normal and malignant breast epithelial cells [15], strongly suggesting that it might play a critical role in differentiation, proliferation, and function of immune cells.Our previous studies show that PIP KO mice have enlarged submandibular lymph nodes and thymic medulla [16]. However, to date, no studies have addressed the contributions of PIP in T-cell responses to either model Ags or infectious agents. Our major aim in the present study is to investigate whether PIP has immunoregulatory function...

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Surface Plasmon Resonance Analysis of gp17, a Natural CD4 Ligand from Human Seminal Plasma Inhibiting Human Immunodeficiency Virus Type‐1 gp120‐Mediated Syncytium Formation

Cited by 45 publications

References 39 publications

Purification and characterization of zinc α2‐glycoprotein‐Prolactin inducible protein complex from human seminal plasma

Purification and characterization of zinc α2‐glycoprotein‐Prolactin inducible protein complex from human seminal plasma

Identification of a CD4 Domain Required for Interleukin-16 Binding and Lymphocyte Activation*

Deficiency of prolactin‐inducible protein leads to impaired Th1 immune response and susceptibility to Leishmania major in mice

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