Correction: Fine Mapping of the Interaction between C4b-Binding Protein and Outer Membrane Proteins LigA and LigB of Pathogenic Leptospira interrogans

Breda, Leandro Carvalho Dantas; Hsieh, Ching-Lin; Valencia, Mónica Marcela Castiblanco; Silva, Ludmila B. da; Barbosa, Angela Silva; Blom, Anna M.; Chang, Yung-Fu; Isaac, Lourdes

doi:10.1371/journal.pntd.0004286

Cited by 3 publications

(3 citation statements)

References 1 publication

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Moreover, these proteins can induce specific antibody production in infected patients 137 . LigA and LigB are able to bind to extracellular matrix components such as fibronectin and Complement regulatory proteins like Factor H 33 and C4b binding protein 71 . Recombinant vaccines prepared with different fragments of LigB and a C‐terminal fragment of LipL32 protected against acute Leptospira infection and lung damage and generated a good antibody response with reduced mortality 138 …”

Section: Development Of Leptospirosis Vaccinesmentioning

confidence: 99%

“…Pathogenic leptospires have developed several strategies to evade the immune system, thus allowing their survival in the host, causing several complications. The main mechanisms of evasion are recruitment of host regulatory proteins of the complement system 33,42,[67][68][69][70][71][72] ; secretion of metalloproteinases, 28,31,73 biofilm formation, 74 changes in LPS composition and expression of catalase. 75 Pathogenic Leptospira also binds in vitro to plasminogen, laminin, fibronectin, thrombin, fibrinogen, extracellular matrix components and certain proteins of the Coagulation System.…”

Section: Immune Evasionmentioning

confidence: 99%

“…137 LigA and LigB are able to bind to extracellular matrix components such as fibronectin and Complement regulatory proteins like Factor H 33 and C4b binding protein. 71 Recombinant vaccines prepared with different fragments of LigB and a C-terminal fragment of LipL32 protected against acute Leptospira infection and lung damage and generated a good antibody response with reduced mortality. 138 Another study investigated the protective capacity of a recombinant vaccine prepared with LipL32 and LigA non-identical fragment (LigANI; domains 7-13), together or separately.…”

Section: Recombinant Protein Vaccinesmentioning

confidence: 99%

See 2 more Smart Citations

Human leptospirosis: In search for a better vaccine

2023

Self Cite

View full text Add to dashboard Cite

Leptospirosis is a neglected disease caused by bacteria of the genus Leptospira and is more prevalent in tropical and subtropical countries. This pathogen infects humans and other animals, responsible for the most widespread zoonosis in the world, estimated to be responsible for 60 000 deaths and 1 million cases per year. To date, commercial vaccines against human leptospirosis are available only in some countries such as Japan, China, Cuba and France. These vaccines prepared with inactivated Leptospira (bacterins) induce a short‐term and serovar‐specific immune response, with strong adverse side effects. To circumvent these limitations, several research groups are investigating new experimental vaccines in order to ensure that they are safe, efficient, and protect against several pathogenic Leptospira serovars, inducing sterilizing immunity. Most of these protocols use attenuated cultures, preparations after LPS removal, recombinant proteins or DNA from pathogenic Leptospira spp. The aim of this review was to highlight several promising vaccine candidates, considering their immunogenicity, presence in different pathogenic Leptospira serovars, their role in virulence or immune evasion and other factors.

show abstract

Section: Development Of Leptospirosis Vaccinesmentioning

confidence: 99%

Section: Immune Evasionmentioning

confidence: 99%

Section: Recombinant Protein Vaccinesmentioning

confidence: 99%

See 1 more Smart Citation

Human leptospirosis: In search for a better vaccine

2023

Self Cite

View full text Add to dashboard Cite

show abstract

Analysis of Immunological Activity of Recombinant Outer Membrane Protein of Fusobacterium Necrophorum

Jia

Wang

Zhang

et al. 2019

IOP Conf. Ser.: Mater. Sci. Eng.

View full text Add to dashboard Cite

To investigate the prokaryotic expression of 93 ku outer membrane protein (OMP) obtained from Fusobacterium necrophorum and the response to immunization and cytotoxicity in mice. The recombinant plasmid pET-28a-OMP was transformed into E. coli BL21 (DE3) competent form, and a recombinant outer membrane protein containing 2 His tags (label size 3.8 ku) was expressed. The mice were immunized as immunization antigens by Freund’s incomplete adjuvant. SDS-PAGE and Western blot analysis showed that the recombinant protein had a molecular weight of about 93 ku. After the immunization, the serum antibody titer of the experimental group was higher, at the same time, in the challenge experiment, the liver has certain toxicity, and the protection rate is 83.3%. The recombinant 93 ku outer membrane protein of Fusobacterium necrophorum has a good immune response level and provides basic data for the study of the subunit vaccine of Fusobacterium necrophorum.

show abstract

Reduced Renal Colonization and Enhanced Protection by Leptospiral Factor H Binding Proteins as a Multisubunit Vaccine against Leptospirosis in Hamsters

et al. 2019

View full text Add to dashboard Cite

Subunit vaccines conferring complete protection against leptospirosis are not currently available. The interactions of factor H binding proteins (FHBPs) on pathogenic leptospires and host factor H are crucial for immune evasion by inhibition of complement-mediated killing. The inhibition of these interactions may be a potential strategy to clear leptospires in the host. This study aimed to evaluate a multisubunit vaccine composed of four known leptospiral FHBPs: LigA domain 7–13 (LigAc), LenA, LcpA, and Lsa23, for its protective efficacy in hamsters. The mono and multisubunit vaccines formulated with LMQ adjuvant, a combination of neutral liposome, monophosphoryl lipid A, and Quillaja saponaria fraction 21, induced high and comparable specific antibody (IgG) production against individual antigens. Hamsters immunized with the multisubunit vaccine showed 60% survival following the challenge by 20 LD50 of Leptospira interrogans serovar Pomona. No significant difference in survival rate and pathological findings of target organs was observed after vaccinations with multisubunit or mono-LigAc vaccines. However, the multisubunit vaccine significantly reduced leptospiral burden in surviving hamsters in comparison with the monosubunit vaccines. Therefore, the multisubunit vaccine conferred partial protection and reduced renal colonization against virulence Leptospira infection in hamsters. Our multisubunit formulation could represent a promising vaccine against leptospirosis.

show abstract

Correction: Fine Mapping of the Interaction between C4b-Binding Protein and Outer Membrane Proteins LigA and LigB of Pathogenic Leptospira interrogans

Cited by 3 publications

References 1 publication

Human leptospirosis: In search for a better vaccine

Human leptospirosis: In search for a better vaccine

Analysis of Immunological Activity of Recombinant Outer Membrane Protein of Fusobacterium Necrophorum

Reduced Renal Colonization and Enhanced Protection by Leptospiral Factor H Binding Proteins as a Multisubunit Vaccine against Leptospirosis in Hamsters

Contact Info

Product

Resources

About