Abstract: Sequential immunization strategies to guide the maturation of antibodies against the human immunodeficiency virus (HIV) are described. The sequential immunization strategies utilize an HIV envelope protein (Env) that binds germline (gl) B cells as a first (prime) immunization and an Env with a functional glycosylated N276 as a second (boost) immunization. The sequential immunization strategies successfully elicit neutralizing antibodies against HIV.

Abstract: The disclosure provides antibodies, antibody fragments, and antibody derivatives that bind to the viral envelope spike protein (S2P) of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), and related compositions, and methods. In some embodiments, the antibodies, antibody fragments, and antibody derivatives bind to an epitope of the receptor binding domain (RBD) of SARS-CoV-2.

Abstract: Sequential immunization strategies to guide the maturation of antibodies against the human immunodeficiency virus (HIV) are described. The sequential immunization strategies utilize an HIV envelope protein (Env) that binds germline (gl) B cells as a first (prime) immunization and an Env with a functional glycosylated N276 as a second (boost) immunization. The sequential immunization strategies successfully elicit neutralizing antibodies against HIV.

Abstract: Engineered and multimerized human immunodeficiency virus (HIV) envelope glycoproteins are described. The envelope glycoproteins can be multimerized using a heptamerization domain such as a C4b binding protein multimerization domain or a ferritin fusion. The engineered and multimerized envelope glycoproteins can derived from glycoprotein 120 (gp120) and can used as an HIV vaccine.

Abstract: Engineered and multimerized human immunodeficiency virus (HIV) envelope glycoproteins are described. The envelope glycoproteins can be multimerized using a heptamerization domain such as a C4b binding protein multimerization domain or a ferritin fusion. The engineered and multimerized envelope glycoproteins can derived from glycoprotein 120 (gp120) and can used as an HIV vaccine.

Abstract: Multimerized human immunodeficiency virus (HIV) envelope glycoproteins are described. The envelope glycoproteins are multimerized Engineered and multimerized human immunodeficiency virus (HIV) envelope glycoproteins are described. The envelope glycoproteins can be multimerized using a heptamerization domain such as a C4b binding protein multimerization domain or a ferritin fusion. The engineered and multimerized envelope glycoproteins can derived from glycoprotein 120 (gp 120) and can used as an HIV vaccine.

Abstract: Multimerized human immunodeficiency virus (HIV) envelope glycoproteins are described. The envelope glycoproteins are multimerized Engineered and multimerized human immunodeficiency virus (HIV) envelope glycoproteins are described. The envelope glycoproteins can be multimerized using a heptamerization domain such as a C4b binding protein multimerization domain or a ferritin fusion. The engineered and multimerized envelope glycoproteins can derived from glycoprotein 120 (gp120) and can used as an HIV vaccine.

Abstract: The invention provides vaccination protocols for administering immunogens to a primate host in order to promote the formation of neutralizing antibodies (NAbs) against primate immunodeficiency viruses. In some embodiments, the vaccination protocols comprise the step of administering to a primate host a first immunogen comprising at least one primate immunodeficiency virus Envelope (env) sequence having a first set of consensus glycosylation sequences, followed by a second immunogen comprising at least one primate immunodeficiency virus env sequence having a second set of consensus glycosylation sequences, wherein the differences between the first set of consensus glycosylation sequences and the second set of consensus glycosylation sequences comprise differences in consensus glycosylation sequences observed in HIV isolates obtained at different time points of a natural infection.

Abstract: In one aspect, the invention provides an HIV envelope heterotrimer comprising at least two different Env glycoprotein monomers. In some heterotrimers, at least two Env glycoprotein monomers are from different HIV isolates, for example, different HIV-1 isolates. Heterotrimers may contain Env glycoprotein monomers from HIV isolates belonging to the same clade or to different clades or both. At least one of the Env glycoprotein monomers in a heterotrimer of the invention may be modified in a way that alters its amino acid composition. In another aspect, the invention provides methods for inducing an immune response in a vertebrate host against HIV or an HIV-infected cell, comprising administering to a vertebrate host a prophylactically or therapeutically effective amount of a composition comprising an HIV envelope heterotrimer.

Abstract: The invention provides vaccination protocols for administering immunogens to a primate host in order to promote the formation of neutralizing antibodies (NAbs) against primate immunodeficiency viruses. In some embodiments, the vaccination protocols comprise the step of administering to a primate host a first immunogen comprising at least one primate immunodeficiency virus Envelope (env) sequence having a first set of consensus glycosylation sequences, followed by a second immunogen comprising at least one primate immunodeficiency virus env sequence having a second set of consensus glycosylation sequences, wherein the differences between the first set of consensus glycosylation sequences and the second set of consensus glycosylation sequences comprise differences in consensus glycosylation sequences observed in HIV isolates obtained at different time points of a natural infection.

Abstract: Methods for immunizing, and immunogen pharmaceutical compositions for eliciting a heterologous immune response to HIV-1 in an animal, preferably a human, are provided, utilizing a modified HIV-1 envelope protein or fragment or DNA encoding a modified HIV-1 envelope protein or fragment, the modified protein having a HIV-1 envelope protein V2 region deletion. A humoral response against heterologous HIV-1 strains is achieved.