The present invention provides a method of making an antibody by identifying a circulating antibody with activity from a subject comprising i) subjecting biological fluid selected from the group consisting of blood, plasma and serum and combinations thereof from the subject to one or more rounds of affinity chromatography to purify the circulating antibody; ii) optionally further subjecting the circulating antibody to isoelectric focusing to purify the circulating antibody based on charge; iii) testing the purified circulating antibody for activity; iv) digesting the purified circulating antibody from parts i) or ii) to create an antibody fragment; v) subjecting the antibody fragment to mass spectrometry to generate a mass assignment and a deduced amino acid sequence of the antibody fragment; vi) comparing the deduced amino acid sequence with an amino acid sequence of an antibody generated from the subject's B-cells to identify an antibody sequence that matches the deduced amino acid sequence; vii) generating an antibody comprising light chain and heavy chain CDR sequences of the B-cell antibody that matches the deducted amino acid sequence of party vi); and viii) testing the antibody of part vii) for activity.

Disclosed is a labeled polypeptide that includes a glutamine residue having a side chain represented by formula (I) below:

##STR00001## (wherein, (C) represents an -carbon of the glutamine residue, X represents a straight chain alkylene group, Y represents a polyethylene glycol chain, Z represents a label, L represents a spacer or an atomic bond, and the polyethylene glycol chain has a molecular weight of 1100 or larger).

The present invention relates to a method of generation of fully functional heavy chain-only antibodies in transgenic mice in response to antigen challenge.

The present invention provides a method of making an antibody by identifying a circulating antibody with activity from a subject comprising i) subjecting biological fluid selected from the group consisting of blood, plasma and serum and combinations thereof from the subject to one or more rounds of affinity chromatography to purify the circulating antibody; ii) optionally further subjecting the circulating antibody to isoelectric focusing to purify the circulating antibody based on charge; iii) testing the purified circulating antibody for activity; iv) digesting the purified circulating antibody from parts i) or ii) to create an antibody fragment; v) subjecting the antibody fragment to mass spectrometry to generate a mass assignment and a deduced amino acid sequence of the antibody fragment; vi) comparing the deduced amino acid sequence with an amino acid sequence of an antibody generated from the subject's B-cells to identify an antibody sequence that matches the deduced amino acid sequence; vii) generating an antibody comprising light chain and heavy chain CDR sequences of the B-cell antibody that matches the deducted amino acid sequence of party vi); and viii) testing the antibody of part vii) for activity.

A method for detecting HIV infection in a mammal is disclosed. The method contains the steps of isolating exosomes from a urine sample of a mammal and detecting the presence of HIV-specific biomarker in said isolated exosomes. A method for diagnosing a mammal with an HIV-associated disease, in particular, HIV-associated nephropathy is also disclosed.

The present invention pertains to the field of T Cell receptors (TCR) identification and clonotyping, and especially concerns particular TCRs identified by clonotyping of a HIV-specific TCR repertoire, or fragments thereof. The invention relates especially to TCRs recognizing Gag peptide located between positions 293-312 in the GAG protein of HIV-1. The present invention further relates to nucleic acid constructs suitable as means for cloning or expressing nucleic acid molecules or TCRs of the invention, such as plasmids, vectors, especially lentiviraltransfer vectors. The invention is of particular interest in the context of therapeutic treatment of human beings seropositive for HIV.

The present application generally relates to methods of genetically modifying a T-cell comprising a chimeric antigen receptor wherein the T-cell lacks a co-receptor for HIV. The application further relates to methods of making a nucleic acid encoding a chimeric antigen receptor, nucleic acids encoding a chimeric antigen receptor, and genetically modified T-cells comprising a chimeric antigen receptor disclosed herein. The application further relates to methods of treating, inhibiting, or ameliorating HIV in a subject including administering to the subject a cell disclosed herein.

Nonlamellar bioresorbable microparticles to which protein substances are bonded, and a method for preparing the microparticles, comprising: (i) preparing the microparticles from at least one bioresorbable polymer without stabilizer and without surfactant; and (ii) bonding the protein substances to the microparticles obtained in step (i) without surfactant.

A method of characterizing a lentivirus, comprising: providing a sample comprising a lentivirus population comprising a fully loaded lentivirus, a partially loaded lentivirus, and/or an empty lentivirus; contacting a substrate with the sample to capture the lentivirus population; contacting the captured lentivirus population with a first fluorescent agent comprising a first fluorescent label and a first binding molecule that binds an envelope protein of the lentivirus, a second fluorescent agent comprising a second fluorescent label and a second binding molecule that binds a capsid protein of the lentivirus, and a third fluorescent agent comprising a third fluorescent label that binds a payload; illuminating the captured lentivirus population with light to excite the fluorescent agents; detecting fluorescent lights emitted from the fluorescent agents at different wavelengths; and characterizing the lentivirus according to the detected fluorescent lights.

An anti-HIV-1 antibody comprising L-CDR1, L-CDR2 and L-CDR3, wherein L-CDR1 is selected from the group consisting of SEQ ID NO: 15, SEQ ID NO: 18, SEQ ID NO: 21, and a sequence that differs from anyone of SEQ ID NOs: 15, 18, or 21 by one or two substitutions, deletions, or additions, the amino acid sequence of L-CDR2 is selected from the group consisting of SEQ ID NO: 16, SEQ ID NO: 19, SEQ ID NO: 22, and a sequence that differs from anyone of SEQ ID NOs: 16, 19, or 22 by one or two substitutions, deletions, or additions, and the amino acid sequence of L-CDR3 is selected from the group consisting of SEQ ID NO: 17, SEQ ID NO: 20, SEQ ID NO: 23, and a sequence that differs from anyone of SEQ ID NOs: 17, 20, or 23 by one or two substitutions, deletions, or additions.